Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Science 23 August 1991:
Vol. 253. no. 5022, pp. 872 - 879
DOI: 10.1126/science.1678899
Prev | Table of Contents | Next

Articles

Science, Vol 253, Issue 5022, 872-879
Copyright © 1991 by American Association for the Advancement of Science

articles

Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein

JL Sussman, M Harel, F Frolow, C Oefner, A Goldman, L Toker, and I Silman

Department of Structural Chemistry, Weizmann Institute of Science, Rehovot, Israel.

The three-dimensional structure of acetylcholinesterase from Torpedo californica electric organ has been determined by x-ray analysis to 2.8 angstrom resolution. The form crystallized is the glycolipid-anchored homodimer that was purified subsequent to solubilization with a bacterial phosphatidylinositol-specific phospholipase C. The enzyme monomer is an alpha/beta protein that contains 537 amino acids. It consists of a 12-stranded mixed beta sheet surrounded by 14 alpha helices and bears a striking resemblance to several hydrolase structures including dienelactone hydrolase, serine carboxypeptidase-II, three neutral lipases, and haloalkane dehalogenase. The active site is unusual because it contains Glu, not Asp, in the Ser-His-acid catalytic triad and because the relation of the triad to the rest of the protein approximates a mirror image of that seen in the serine proteases. Furthermore, the active site lies near the bottom of a deep and narrow gorge that reaches halfway into the protein. Modeling of acetylcholine binding to the enzyme suggests that the quaternary ammonium ion is bound not to a negatively charged "anionic" site, but rather to some of the 14 aromatic residues that line the gorge.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Limiting Role of Protein Disulfide Isomerase in the Expression of Collagen-tailed Acetylcholinesterase Forms in Muscle.
C. A. Ruiz and R. L. Rotundo (2009)
J. Biol. Chem. 284, 31753-31763
   Abstract »    Full Text »    PDF »
SLITHER: a web server for generating contiguous conformations of substrate molecules entering into deep active sites of proteins or migrating through channels in membrane transporters.
P.-H. Lee, K.-L. Kuo, P.-Y. Chu, E. M. Liu, and J.-H. Lin (2009)
Nucleic Acids Res. 37, W559-W564
   Abstract »    Full Text »    PDF »
The Cholinesterase-like Domain, Essential in Thyroglobulin Trafficking for Thyroid Hormone Synthesis, Is Required for Protein Dimerization.
J. Lee, X. Wang, B. Di Jeso, and P. Arvan (2009)
J. Biol. Chem. 284, 12752-12761
   Abstract »    Full Text »    PDF »
Aging-Resistant Organophosphate Bioscavenger Based on Polyethylene Glycol-Conjugated F338A Human Acetylcholinesterase.
O. Mazor, O. Cohen, C. Kronman, L. Raveh, D. Stein, A. Ordentlich, and A. Shafferman (2008)
Mol. Pharmacol. 74, 755-763
   Abstract »    Full Text »    PDF »
Shoot-and-Trap: Use of specific x-ray damage to study structural protein dynamics by temperature-controlled cryo-crystallography.
J.-P. Colletier, D. Bourgeois, B. Sanson, D. Fournier, J. L. Sussman, I. Silman, and M. Weik (2008)
PNAS 105, 11742-11747
   Abstract »    Full Text »    PDF »
Effect of L-carnitine administration on the modulated rat brain protein concentration, acetylcholinesterase, Na+K+-ATPase and Mg2+-ATPase activities induced by forced swimming.
T Tsakiris, P Angelogianni, C Tesseromatis, S Tsakiris, and K H Schulpis (2008)
Br. J. Sports Med. 42, 367-372
   Abstract »    Full Text »    PDF »
Cation-{pi} Interactions Involving Aromatic Amino Acids.
D. A. Dougherty (2007)
J. Nutr. 137, 1504S-1508S
   Abstract »    Full Text »    PDF »
The Kinetics of Inhibition of Human Acetylcholinesterase and Butyrylcholinesterase by Two Series of Novel Carbamates.
E. Groner, Y. Ashani, D. Schorer-Apelbaum, J. Sterling, Y. Herzig, and M. Weinstock (2007)
Mol. Pharmacol. 71, 1610-1617
   Abstract »    Full Text »    PDF »
Substrate and Product Trafficking through the Active Center Gorge of Acetylcholinesterase Analyzed by Crystallography and Equilibrium Binding.
Y. Bourne, Z. Radic, G. Sulzenbacher, E. Kim, P. Taylor, and P. Marchot (2006)
J. Biol. Chem. 281, 29256-29267
   Abstract »    Full Text »    PDF »
Butyrylcholinesterase attenuates amyloid fibril formation in vitro.
S. Diamant, E. Podoly, A. Friedler, H. Ligumsky, O. Livnah, and H. Soreq (2006)
PNAS 103, 8628-8633
   Abstract »    Full Text »    PDF »
Pseudomonas aeruginosa LD-Carboxypeptidase, a Serine Peptidase with a Ser-His-Glu Triad and a Nucleophilic Elbow.
H. J. Korza and M. Bochtler (2005)
J. Biol. Chem. 280, 40802-40812
   Abstract »    Full Text »    PDF »
Dissection of Synapse Induction by Neuroligins: EFFECT OF A NEUROLIGIN MUTATION ASSOCIATED WITH AUTISM.
A. A. Chubykin, X. Liu, D. Comoletti, I. Tsigelny, P. Taylor, and T. C. Sudhof (2005)
J. Biol. Chem. 280, 22365-22374
   Abstract »    Full Text »    PDF »
The Crystal Structure of the Complex of the Anticancer Prodrug 7-Ethyl-10-[4-(1-piperidino)-1-piperidino]-carbonyloxycamptothecin (CPT-11) with Torpedo californica Acetylcholinesterase Provides a Molecular Explanation for Its Cholinergic Action.
M. Harel, J. L. Hyatt, B. Brumshtein, C. L. Morton, K. J. P. Yoon, R. M. Wadkins, I. Silman, J. L. Sussman, and P. M. Potter (2005)
Mol. Pharmacol. 67, 1874-1881
   Abstract »    Full Text »    PDF »
Mutational Analysis of nocK and nocL in the Nocardicin A Producer Nocardia uniformis.
W. L. Kelly and C. A. Townsend (2005)
J. Bacteriol. 187, 739-746
   Abstract »    Full Text »    PDF »
Determinants of the t Peptide Involved in Folding, Degradation, and Secretion of Acetylcholinesterase.
C. Falasca, N. Perrier, J. Massoulie, and S. Bon (2005)
J. Biol. Chem. 280, 878-886
   Abstract »    Full Text »    PDF »
Compound library development guided by protein structure similarity clustering and natural product structure.
M. A. Koch, L.-O. Wittenberg, S. Basu, D. A. Jeyaraj, E. Gourzoulidou, K. Reinecke, A. Odermatt, and H. Waldmann (2004)
PNAS 101, 16721-16726
   Abstract »    Full Text »    PDF »
Disorder-associated mutations lead to functional inactivation of neuroligins.
B. Chih, S. K. Afridi, L. Clark, and P. Scheiffele (2004)
Hum. Mol. Genet. 13, 1471-1477
   Abstract »    Full Text »    PDF »
Acrylodan-conjugated Cysteine Side Chains Reveal Conformational State and Ligand Site Locations of the Acetylcholine-binding Protein.
R. E. Hibbs, T. T. Talley, and P. Taylor (2004)
J. Biol. Chem. 279, 28483-28491
   Abstract »    Full Text »    PDF »
Nanosecond Dynamics of Acetylcholinesterase Near the Active Center Gorge.
A. E. Boyd, C. S. Dunlop, L. Wong, Z. Radic, P. Taylor, and D. A. Johnson (2004)
J. Biol. Chem. 279, 26612-26618
   Abstract »    Full Text »    PDF »
The Acetylcholinesterase Homology Region Is Essential for Normal Conformational Maturation and Secretion of Thyroglobulin.
Y.-n. Park and P. Arvan (2004)
J. Biol. Chem. 279, 17085-17089
   Abstract »    Full Text »    PDF »
Freeze-frame inhibitor captures acetylcholinesterase in a unique conformation.
Y. Bourne, H. C. Kolb, Z. Radic, K. B. Sharpless, P. Taylor, and P. Marchot (2004)
PNAS 101, 1449-1454
   Abstract »    Full Text »    PDF »
Differentiation between Acetylcholinesterase and the Organophosphate-inhibited Form Using Antibodies and the Correlation of Antibody Recognition with Reactivation Mechanism and Rate.
K. M. George, T. Schule, L. E. Sandoval, L. L. Jennings, P. Taylor, and C. M. Thompson (2003)
J. Biol. Chem. 278, 45512-45518
   Abstract »    Full Text »    PDF »
Crystal Structure of Human Butyrylcholinesterase and of Its Complexes with Substrate and Products.
Y. Nicolet, O. Lockridge, P. Masson, J. C. Fontecilla-Camps, and F. Nachon (2003)
J. Biol. Chem. 278, 41141-41147
   Abstract »    Full Text »    PDF »
Inhibitors Tethered Near the Acetylcholinesterase Active Site Serve as Molecular Rulers of the Peripheral and Acylation Sites.
J. L. Johnson, B. Cusack, T. F. Hughes, E. H. McCullough, A. Fauq, P. Romanovskis, A. F. Spatola, and T. L. Rosenberry (2003)
J. Biol. Chem. 278, 38948-38955
   Abstract »    Full Text »    PDF »
Cholinesterase Reactivation in Vivo with a Novel Bis-Oxime Optimized by Computer-Aided Design.
P. I. Hammond, C. Kern, F. Hong, T. M. Kollmeyer, Y.-P. Pang, and S. Brimijoin (2003)
J. Pharmacol. Exp. Ther. 307, 190-196
   Abstract »    Full Text »    PDF »
Nanosecond Dynamics of the Mouse Acetylcholinesterase Cys69-Cys96 Omega Loop.
J. Shi, K. Tai, J. A. McCammon, P. Taylor, and D. A. Johnson (2003)
J. Biol. Chem. 278, 30905-30911
   Abstract »    Full Text »    PDF »
A long insertion reverts the functional effect of a substitution in acetylcholinesterase.
F. Villatte, H. Schulze, R.D. Schmid, and T.T. Bachmann (2003)
Protein Eng. Des. Sel. 16, 463-465
   Abstract »    Full Text »    PDF »
Structure of Human Carnitine Acetyltransferase. MOLECULAR BASIS FOR FATTY ACYL TRANSFER.
D. Wu, L. Govindasamy, W. Lian, Y. Gu, T. Kukar, M. Agbandje-McKenna, and R. McKenna (2003)
J. Biol. Chem. 278, 13159-13165
   Abstract »    Full Text »    PDF »
Observation of an Arsenic Adduct in an Acetyl Esterase Crystal Structure.
X. Zhu, N. A. Larsen, A. Basran, N. C. Bruce, and I. A. Wilson (2003)
J. Biol. Chem. 278, 2008-2014
   Abstract »    Full Text »    PDF »
Mapping and Molecular Modeling of S-Adenosyl-L-methionine Binding Sites in N-Methyltransferase Domains of the Multifunctional Polypeptide Cyclosporin Synthetase.
T. Velkov and A. Lawen (2003)
J. Biol. Chem. 278, 1137-1148
   Abstract »    Full Text »    PDF »
Mouse Liver and Kidney Carboxylesterase (M-LK) Rapidly Hydrolyzes Antitumor Prodrug Irinotecan and the N-Terminal Three Quarter Sequence Determines Substrate Selectivity.
M. Xie, D. Yang, M. Wu, B. Xue, and B. Yan (2003)
Drug Metab. Dispos. 31, 21-27
   Abstract »    Full Text »    PDF »
Inhibitors of Different Structure Induce Distinguishing Conformations in the Omega Loop, Cys69-Cys96, of Mouse Acetylcholinesterase.
J. Shi, Z. Radic', and P. Taylor (2002)
J. Biol. Chem. 277, 43301-43308
   Abstract »    Full Text »    PDF »
Contributions of the non-{alpha} subunit residues (loop D) to agonist binding and channel gating in the muscle nicotinic acetylcholine receptor.
G. Akk (2002)
J. Physiol. 544, 695-705
   Abstract »    Full Text »    PDF »
Tryptophan Fluorescence Reveals Conformational Changes in the Acetylcholine Binding Protein.
S. B. Hansen, Z. Radic', T. T. Talley, B. E. Molles, T. Deerinck, I. Tsigelny, and P. Taylor (2002)
J. Biol. Chem. 277, 41299-41302
   Abstract »    Full Text »    PDF »
Acetylcholinesterase Activity and Biogenic Amines in Phenylketonuria.
K. H. Schulpis, G. A. Karikas, J. Tjamouranis, H. Michelakakis, and S. Tsakiris (2002)
Clin. Chem. 48, 1794-1796
   Full Text »    PDF »
Extremely Stable and Versatile Carboxylesterase from a Hyperthermophilic Archaeon.
Y. Hotta, S. Ezaki, H. Atomi, and T. Imanaka (2002)
Appl. Envir. Microbiol. 68, 3925-3931
   Abstract »    Full Text »    PDF »
Human and Rodent Carboxylesterases: Immunorelatedness, Overlapping Substrate Specificity, Differential Sensitivity to Serine Enzyme Inhibitors, and Tumor-Related Expression.
M. Xie, D. Yang, L. Liu, B. Xue, and B. Yan (2002)
Drug Metab. Dispos. 30, 541-547
   Abstract »    Full Text »    PDF »
Acetylcholinesterase engineering for detection of insecticide residues.
Y. Boublik, P. Saint-Aguet, A. Lougarre, M. Arnaud, F. Villatte, S. Estrada-Mondaca, and D. Fournier (2002)
Protein Eng. Des. Sel. 15, 43-50
   Abstract »    Full Text »    PDF »
Reversibly Bound and Covalently Attached Ligands Induce Conformational Changes in the Omega Loop, Cys69-Cys96, of Mouse Acetylcholinesterase.
J. Shi, A. E. Boyd, Z. Radic, and P. Taylor (2001)
J. Biol. Chem. 276, 42196-42204
   Abstract »    Full Text »    PDF »
Incorporation of caged cysteine and caged tyrosine into a transmembrane segment of the nicotinic ACh receptor.
K. D. Philipson, J. P. Gallivan, G. S. Brandt, D. A. Dougherty, and H. A. Lester (2001)
Am J Physiol Cell Physiol 281, C195-C206
   Abstract »    Full Text »    PDF »
Force Spectroscopy between Acetylcholine and Single Acetylcholinesterase Molecules and the Effects of Inhibitors and Reactivators Studied by Atomic Force Microscopy.
Z. Yingge, B. Chunli, W. Chen, and Z. Delu (2001)
J. Pharmacol. Exp. Ther. 297, 798-803
   Abstract »    Full Text »
Interactions of the Organophosphates Paraoxon and Methyl Paraoxon with Mouse Brain Acetylcholinesterase.
S. A. Kardos and L. G. Sultatos (2000)
Toxicol. Sci. 58, 118-126
   Abstract »    Full Text »    PDF »
Analysis of the psychrotolerant property of hormone-sensitive lipase through site-directed mutagenesis.
H. Laurell, J. A. Contreras, I. Castan, D. Langin, and C. Holm (2000)
Protein Eng. Des. Sel. 13, 711-717
   Abstract »    Full Text »    PDF »
Inactivation Studies of Acetylcholinesterase with Phenylmethylsulfonyl Fluoride.
D. Kraut, H. Goff, R. K. Pai, N. A. Hosea, I. Silman, J. L. Sussman, P. Taylor, and J. G. Voet (2000)
Mol. Pharmacol. 57, 1243-1248
   Abstract »    Full Text »
Exploration of the Drosophila Acetylcholinesterase Substrate Activation Site Using a Reversible Inhibitor (Triton X-100) and Mutated Enzymes.
V. Marcel, S. Estrada-Mondaca, F. Magne, J. Stojan, A. Klaebe, and D. Fournier (2000)
J. Biol. Chem. 275, 11603-11609
   Abstract »    Full Text »    PDF »
Huprine X is a Novel High-Affinity Inhibitor of Acetylcholinesterase That Is of Interest for Treatment of Alzheimer's Disease.
P. Camps, B. Cusack, W. D. Mallender, R. E. Achab, J. Morral, D. Muñoz-Torrero, and T. L. Rosenberry (2000)
Mol. Pharmacol. 57, 409-417
   Abstract »    Full Text »
From the Cover: Specific chemical and structural damage to proteins produced by synchrotron radiation.
M. Weik, R. B. G. Ravelli, G. Kryger, S. McSweeney, M. L. Raves, M. Harel, P. Gros, I. Silman, J. Kroon, and J. L. Sussman (2000)
PNAS 97, 623-628
   Abstract »    Full Text »    PDF »
Territrem B, a Tremorgenic Mycotoxin That Inhibits Acetylcholinesterase with a Noncovalent yet Irreversible Binding Mechanism.
J.-W. Chen, Y.-L. Luo, M.-J. Hwang, F.-C. Peng, and K.-H. Ling (1999)
J. Biol. Chem. 274, 34916-34923
   Abstract »    Full Text »    PDF »
A structural view of evolutionary divergence.
B. Spiller, A. Gershenson, F. H. Arnold, and R. C. Stevens (1999)
PNAS 96, 12305-12310
   Abstract »    Full Text »    PDF »
Conformational Flexibility of the Acetylcholinesterase Tetramer Suggested by X-ray Crystallography.
Y. Bourne, J. Grassi, P. E. Bougis, and P. Marchot (1999)
J. Biol. Chem. 274, 30370-30376
   Abstract »    Full Text »    PDF »
The Binding Sites of Inhibitory Monoclonal Antibodies on Acetylcholinesterase. IDENTIFICATION OF A NOVEL REGULATORY SITE AT THE PUTATIVE "BACK DOOR".
S. Simon, A. Le Goff, Y. Frobert, J. Grassi, and J. Massoulie (1999)
J. Biol. Chem. 274, 27740-27746
   Abstract »    Full Text »    PDF »
Cation-pi interactions in structural biology.
J. P. Gallivan and D. A. Dougherty (1999)
PNAS 96, 9459-9464
   Abstract »    Full Text »    PDF »
Knowledge-based modeling of the serine protease triad into non-proteases.
P. Iengar and C. Ramakrishnan (1999)
Protein Eng. Des. Sel. 12, 649-656
   Abstract »    Full Text »    PDF »
Effect of Mutations within the Peripheral Anionic Site on the Stability of Acetylcholinesterase.
N. Morel, S. Bon, H. M. Greenblatt, D. Van Belle, S. J. Wodak, J. L. Sussman, J. Massoulié, and I. Silman (1999)
Mol. Pharmacol. 55, 982-992
   Abstract »    Full Text »
Review : The Vicious Circle of Stress and Anticholinesterase Responses.
D. Kaufer, A. Friedman, and H. Soreq (1999)
Neuroscientist 5, 173-183
   Abstract »    PDF »
Cloning, Expression, and Properties of a Nonneuronal Secreted Acetylcholinesterase from the Parasitic Nematode Nippostrongylus brasiliensis.
A. S. Hussein, M. R. Chacon, A. M. Smith, R. Tosado-Acevedo, and M. E. Selkirk (1999)
J. Biol. Chem. 274, 9312-9319
   Abstract »    Full Text »    PDF »
The Anticancer Prodrug CPT-11 Is a Potent Inhibitor of Acetylcholinesterase but Is Rapidly Catalyzed to SN-38 by Butyrylcholinesterase.
C. L. Morton, R. M. Wadkins, M. K. Danks, and P. M. Potter (1999)
Cancer Res. 59, 1458-1463
   Abstract »    Full Text »    PDF »
Organophosphorylation of Acetylcholinesterase in the Presence of Peripheral Site Ligands. DISTINCT EFFECTS OF PROPIDIUM AND FASCICULIN.
W. D. Mallender, T. Szegletes, and T. L. Rosenberry (1999)
J. Biol. Chem. 274, 8491-8499
   Abstract »    Full Text »    PDF »
Crystal Structure of Mouse Acetylcholinesterase. A PERIPHERAL SITE-OCCLUDING LOOP IN A TETRAMERIC ASSEMBLY.
Y. Bourne, P. Taylor, P. E. Bougis, and P. Marchot (1999)
J. Biol. Chem. 274, 2963-2970
   Abstract »    Full Text »    PDF »
A Molecular Basis for the Different Local Anesthetic Affinities of Resting Versus Open and Inactivated States of the Sodium Channel.
H.-L. Li, A. Galue, L. Meadows, and D. S. Ragsdale (1999)
Mol. Pharmacol. 55, 134-141
   Abstract »    Full Text »
From ab initio quantum mechanics to molecular neurobiology: A cation-pi binding site in the nicotinic receptor.
W. Zhong, J. P. Gallivan, Y. Zhang, L. Li, H. A. Lester, and D. A. Dougherty (1998)
PNAS 95, 12088-12093
   Abstract »    Full Text »    PDF »
Ionophores and receptors using cation-pi interactions: Collarenes.
H. S. Choi, S. B. Suh, S. J. Cho, and K. S. Kim (1998)
PNAS 95, 12094-12099
   Abstract »    Full Text »    PDF »
A single amino acid change in the acetylcholinesterase-like domain of thyroglobulin causes congenital goiter with hypothyroidism in the cog/cog mouse: A model of human endoplasmic reticulum storage diseases.
P. S. Kim, S. A. Hossain, Y.-N. Park, I. Lee, S.-E. Yoo, and P. Arvan (1998)
PNAS 95, 9909-9913
   Abstract »    Full Text »    PDF »
Mutations causing muscle weakness.
J. Lindstrom (1998)
PNAS 95, 9070-9071
   Full Text »    PDF »
Conformation gating as a mechanism for enzyme specificity.
H.-X. Zhou, S. T. Wlodek, and J. A. McCammon (1998)
PNAS 95, 9280-9283
   Abstract »    Full Text »    PDF »
Two Domains of the Beta Subunit of Neuronal Nicotinic Acetylcholine Receptors Contribute to the Affinity of Substance P.
G. A. Stafford, R. E. Oswald, A. Figl, B. N. Cohen, and G. A. Weiland (1998)
J. Pharmacol. Exp. Ther. 286, 619-626
   Abstract »    Full Text »
Functional Characteristics of the Oxyanion Hole in Human Acetylcholinesterase.
A. Ordentlich, D. Barak, C. Kronman, N. Ariel, Y. Segall, B. Velan, and A. Shafferman (1998)
J. Biol. Chem. 273, 19509-19517
   Abstract »    Full Text »    PDF »
Monoterpene Synthases from Common Sage (Salvia officinalis). cDNA ISOLATION, CHARACTERIZATION, AND FUNCTIONAL EXPRESSION OF (+)-SABINENE SYNTHASE, 1,8-CINEOLE SYNTHASE, AND (+)-BORNYL DIPHOSPHATE SYNTHASE.
M. L. Wise, T. J. Savage, E. Katahira, and R. Croteau (1998)
J. Biol. Chem. 273, 14891-14899
   Abstract »    Full Text »    PDF »
Distinctions in Agonist and Antagonist Specificity Conferred by Anionic Residues of the Nicotinic Acetylcholine Receptor.
H. Osaka, N. Sugiyama, and P. Taylor (1998)
J. Biol. Chem. 273, 12758-12765
   Abstract »    Full Text »    PDF »
Acetylcholinesterase Enhances Neurite Growth and Synapse Development through Alternative Contributions of Its Hydrolytic Capacity, Core Protein, and Variable C Termini.
M. Sternfeld, G.-l. Ming, H.-j. Song, K. Sela, R. Timberg, M.-m. Poo, and H. Soreq (1998)
J. Neurosci. 18, 1240-1249
   Abstract »    Full Text »    PDF »
Mutagenesis of the NS3 Protease of Dengue Virus Type 2.
R. P. C. Valle and B. Falgout (1998)
J. Virol. 72, 624-632
   Abstract »    Full Text »    PDF »
Cloning and Expression of Acetylcholinesterase from Electrophorus. SPLICING PATTERN OF THE 3' EXONS IN VIVO AND IN TRANSFECTED MAMMALIAN CELLS.
S. Simon and J. Massoulie (1997)
J. Biol. Chem. 272, 33045-33055
   Abstract »    Full Text »    PDF »
Electrostatic Influence on the Kinetics of Ligand Binding to Acetylcholinesterase. DISTINCTIONS BETWEEN ACTIVE CENTER LIGANDS AND FASCICULIN.
Z. Radic, P. D. Kirchhoff, D. M. Quinn, J. A. McCammon, and P. Taylor (1997)
J. Biol. Chem. 272, 23265-23277
   Abstract »    Full Text »    PDF »
Regiospecificity and Catalytic Triad of Lysophospholipase I.
A. Wang, R. Loo, Z. Chen, and E. A. Dennis (1997)
J. Biol. Chem. 272, 22030-22036
   Abstract »    Full Text »    PDF »
Microsecond atomic force sensing of protein conformational dynamics: Implications for the primary light-induced events in bacteriorhodopsin.
I. Rousso, E. Khachatryan, Y. Gat, I. Brodsky, M. Ottolenghi, M. Sheves, and A. Lewis (1997)
PNAS 94, 7937-7941
   Abstract »    Full Text »    PDF »
A single amino acid substitution converts a carboxylesterase to an organophosphorus hydrolase and confers insecticide resistance on a blowfly.
R. D. Newcomb, P. M. Campbell, D. L. Ollis, E. Cheah, R. J. Russell, and J. G. Oakeshott (1997)
PNAS 94, 7464-7468
   Abstract »    Full Text »    PDF »
Tyrosine 140 of the gamma -Aminobutyric Acid Transporter GAT-1 Plays a Critical Role in Neurotransmitter Recognition.
Y. Bismuth, M. P. Kavanaugh, and B. I. Kanner (1997)
J. Biol. Chem. 272, 16096-16102
   Abstract »    Full Text »    PDF »
Expression and Activity of Mutants of Fasciculin, a Peptidic Acetylcholinesterase Inhibitor from Mamba Venom.
P. Marchot, C. N. Prowse, J. Kanter, S. Camp, E. J. Ackermann, P. E. Bougis, and P. Taylor (1997)
J. Biol. Chem. 272, 3502-3510
   Abstract »    Full Text »    PDF »
Hormone-sensitive Lipase Is Structurally Related to Acetylcholinesterase, Bile Salt-stimulated Lipase, and Several Fungal Lipases. BUILDING OF A THREE-DIMENSIONAL MODEL FOR THE CATALYTIC DOMAIN OF HORMONE-SENSITIVE LIPASE.
J. A. Contreras, M. Karlsson, T. Osterlund, H. Laurell, A. Svensson, and C. Holm (1996)
J. Biol. Chem. 271, 31426-31430
   Abstract »    Full Text »    PDF »
Anionic Residue in the alpha -Subunit of the Nicotinic Acetylcholine Receptor Contributing to Subunit Assembly and Ligand Binding.
N. Sugiyama, A. E. Boyd, and P. Taylor (1996)
J. Biol. Chem. 271, 26575-26581
   Abstract »    Full Text »    PDF »
Highly Potent, Selective, and Low Cost Bis-tetrahydroaminacrine Inhibitors of Acetylcholinesterase. STEPS TOWARD NOVEL DRUGS FOR TREATING ALZHEIMER'S DISEASE.
Y.-P. Pang, P. Quiram, T. Jelacic, F. Hong, and S. Brimijoin (1996)
J. Biol. Chem. 271, 23646-23649
   Abstract »    Full Text »    PDF »
Identification of a C-reactive Protein Binding Site in Two Hepatic Carboxylesterases Capable of Retaining C-reactive Protein within the Endoplasmic Reticulum.
C. C. Yue, J. Muller-Greven, P. Dailey, G. Lozanski, V. Anderson, and S. Macintyre (1996)
J. Biol. Chem. 271, 22245-22250
   Abstract »    Full Text »    PDF »
Crystal Structure of L-2-Haloacid Dehalogenase from Pseudomonas sp. YL. AN alpha /beta HYDROLASE STRUCTURE THAT IS DIFFERENT FROM THE alpha /beta HYDROLASE FOLD.
T. Hisano, Y. Hata, T. Fujii, J.-Q. Liu, T. Kurihara, N. Esaki, and K. Soda (1996)
J. Biol. Chem. 271, 20322-20330
   Abstract »    Full Text »    PDF »
Identification of Essential Residues for the Catalytic Function of 85-kDa Cytosolic Phospholipase A2. PROBING THE ROLE OF HISTIDINE, ASPARTIC ACID, CYSTEINE, AND ARGININE.
R. T. Pickard, X. G. Chiou, B. A. Strifler, M. R. DeFelippis, P. A. Hyslop, A. L. Tebbe, Y. K. Yee, L. J. Reynolds, E. A. Dennis, R. M. Kramer, et al. (1996)
J. Biol. Chem. 271, 19225-19231
   Abstract »    Full Text »    PDF »
Proposed Ligand Binding Site of the Transmembrane Receptor for Neurotensin(8-13).
Y.-P. Pang, B. Cusack, K. Groshan, and E. Richelson (1996)
J. Biol. Chem. 271, 15060-15068
   Abstract »    Full Text »    PDF »
Cloning and Expression of Acetylcholinesterase from Bungarus fasciatus Venom. A NEW TYPE OF COOH-TERMINAL DOMAIN; INVOLVEMENT OF A POSITIVELY CHARGED RESIDUE IN THE PERIPHERAL SITE.
X. Cousin, S. Bon, N. Duval, J. Massoulie, and C. Bon (1996)
J. Biol. Chem. 271, 15099-15108
   Abstract »    Full Text »    PDF »
The Architecture of Human Acetylcholinesterase Active Center Probed by Interactions with Selected Organophosphate Inhibitors.
A. Ordentlich, D. Barak, C. Kronman, N. Ariel, Y. Segall, B. Velan, and A. Shafferman (1996)
J. Biol. Chem. 271, 11953-11962
   Abstract »    Full Text »    PDF »
Role of Aromatic Transmembrane Residues of the [IMAGE]-Opioid Receptor in Ligand Recognition.
K. Befort, L. Tabbara, D. Kling, B. Maigret, and B. L. Kieffer (1996)
J. Biol. Chem. 271, 10161-10168
   Abstract »    Full Text »    PDF »
Structures, Alternative Splicing, and Neurexin Binding of Multiple Neuroligins.
K. Ichtchenko, T. Nguyen, and T. C. Südhof (1996)
J. Biol. Chem. 271, 2676-2682
   Abstract »    Full Text »    PDF »
Review : Neuropsychopathological changes by organophosphorus compounds -- a review.
P. Eyer (1995)
Human and Experimental Toxicology 14, 857-864
   Abstract »    PDF »
Allosteric Control of Acetylcholinesterase Catalysis by Fasciculin.
Z. Radić, D. M. Quinn, D. C. Vellom, S. Camp, and P. Taylor (1995)
J. Biol. Chem. 270, 20391-20399
   Abstract »    Full Text »    PDF »
Fasciculin 2 Binds to the Peripheral Site on Acetylcholinesterase and Inhibits Substrate Hydrolysis by Slowing a Step Involving Proton Transfer during Enzyme Acylation.
J. Eastman, E. J. Wilson, C. Cerveñansky, and T. L. Rosenberry (1995)
J. Biol. Chem. 270, 19694-19701
   Abstract »    Full Text »    PDF »
Classical electrostatics in biology and chemistry.
B Honig and A Nicholls (1995)
Science 268, 1144-1149
   Abstract »    PDF »
Nicotinic receptor binding site probed with unnatural amino acid incorporation in intact cells.
M. Nowak, P. Kearney, Sampson JR, M. Saks, C. Labarca, S. Silverman, W Zhong, J Thorson, J. Abelson, N Davidson, et al. (1995)
Science 268, 439-442
   Abstract »    PDF »
Amino Acid Residues Controlling Reactivation of Organophosphonyl Conjugates of Acetylcholinesterase by Mono- and Bisquaternary Oximes.
Y. Ashani, Z. Radic, I. Tsigelny, D. C. Vellom, N. A. Pickering, D. M. Quinn, B. P. Doctor, and P. Taylor (1995)
J. Biol. Chem. 270, 6370-6380
   Abstract »    Full Text »    PDF »
The Activity of an Endoplasmic Reticulum-localized Pool of Acetylcholinesterase Is Modulated by Heat Shock.
J. Eichler and I. Silman (1995)
J. Biol. Chem. 270, 4466-4472
   Abstract »    Full Text »    PDF »
Contribution of Aromatic Moieties of Tyrosine 133 and of the Anionic Subsite Tryptophan 86 to Catalytic Efficiency and Allosteric Modulation of Acetylcholinesterase.
A. Ordentlich, D. Barak, C. Kronman, N. Ariel, Y. Segall, B. Velan, and A. Shafferman (1995)
J. Biol. Chem. 270, 2082-2091
   Abstract »    Full Text »    PDF »
Open "back door" in a molecular dynamics simulation of acetylcholinesterase.
M. Gilson, T. Straatsma, J. McCammon, D. Ripoll, C. Faerman, P. Axelsen, I Silman, and J. Sussman (1994)
Science 263, 1276-1278
   Abstract »    PDF »
Crystal structure of neocarzinostatin, an antitumor protein-chromophore complex.
K. Kim, B. Kwon, A. Myers, and D. Rees (1993)
Science 262, 1042-1046
   Abstract »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)