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Science 9 October 1992:
Vol. 258. no. 5080, pp. 307 - 310
DOI: 10.1126/science.1384130
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Articles

Science, Vol 258, Issue 5080, 307-310
Copyright © 1992 by American Association for the Advancement of Science

articles

Acetylcholine receptor channel structure probed in cysteine-substitution mutants

MH Akabas, DA Stauffer, M Xu, and A Karlin

Department of Physiology, College of Physicians and Surgeons, Columbia University, New York, NY 10032.

In order to understand the structural bases of ion conduction, ion selectivity, and gating in the nicotinic acetylcholine receptor, mutagenesis and covalent modification were combined to identify the amino acid residues that line the channel. The side chains of alternate residues--Ser248, Leu250, Ser252, and Thr254--in M2, a membrane-spanning segment of the alpha subunit, are exposed in the closed channel. Thus alpha 248-254 probably forms a beta strand, and the gate is closer to the cytoplasmic end of the channel than any of these residues. On channel opening, Leu251 is also exposed. These results lead to a revised view of the closed and open channel structures.


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Probing the Role of a Conserved M1 Proline Residue in 5-Hydroxytryptamine3 Receptor Gating.
H. Dang, P. M. England, S. S. Farivar, D. A. Dougherty, and H. A. Lester (2000)
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   Abstract »    Full Text »    PDF »
The Reactivity of the gamma -Aminobutyric Acid Transporter GAT-1 toward Sulfhydryl Reagents Is Conformationally Sensitive. IDENTIFICATION OF A MAJOR TARGET RESIDUE.
V. Golovanevsky and B. I. Kanner (1999)
J. Biol. Chem. 274, 23020-23026
   Abstract »    Full Text »    PDF »
Nicotinic Acetylcholine Receptors Assembled from the alpha 7 and beta 3 Subunits.
E. Palma, L. Maggi, B. Barabino, F. Eusebi, and M. Ballivet (1999)
J. Biol. Chem. 274, 18335-18340
   Abstract »    Full Text »    PDF »
Transmembrane Domain I Contributes to the Permeation Pathway for Serotonin and Ions in the Serotonin Transporter.
E. L. Barker, K. R. Moore, F. Rakhshan, and R. D. Blakely (1999)
J. Neurosci. 19, 4705-4717
   Abstract »    Full Text »    PDF »
Phe310 in Transmembrane VI of the alpha 1B-Adrenergic Receptor Is a Key Switch Residue Involved in Activation and Catecholamine Ring Aromatic Bonding.
S. Chen, M. Xu, F. Lin, D. Lee, P. Riek, and R. M. Graham (1999)
J. Biol. Chem. 274, 16320-16330
   Abstract »    Full Text »    PDF »
Investigation of the Extracellular Accessibility of the Connecting Loop between Membrane Domains I and II of the Bradykinin B2 Receptor.
U. Quitterer, E. Zaki, and S. AbdAlla (1999)
J. Biol. Chem. 274, 14773-14778
   Abstract »    Full Text »    PDF »
Cysteine scanning analysis of the IFM cluster in the inactivation gate of a human heart sodium channel.
I. Deschenes, E. Trottier, and M. Chahine (1999)
Cardiovasc Res 42, 521-529
   Abstract »    Full Text »    PDF »
The Nicotinic alpha 4 Receptor Subunit Contributes to the Lining of the Ion Channel Pore When Expressed with the 5-HT3 Receptor Subunit.
S. Kriegler, S. Sudweeks, and J. L. Yakel (1999)
J. Biol. Chem. 274, 3934-3936
   Abstract »    Full Text »    PDF »
Identification of Residues Lining the Translocation Pore of Human AE1, Plasma Membrane Anion Exchange Protein.
X.-B. Tang, M. Kovacs, D. Sterling, and J. R. Casey (1999)
J. Biol. Chem. 274, 3557-3564
   Abstract »    Full Text »    PDF »
Modulation of recombinant human cardiac L-type Ca2+ channel {alpha}1C subunits by redox agents and hypoxia.
I M Fearon, A C V Palmer, A J Balmforth, S G Ball, G Varadi, and C Peers (1999)
J. Physiol. 514, 629-637
   Abstract »    Full Text »    PDF »
pH-dependent Gating of ROMK (Kir1.1) Channels Involves Conformational Changes in Both N and C Termini.
U. Schulte, H. Hahn, H. Wiesinger, J. P. Ruppersberg, and B. Fakler (1998)
J. Biol. Chem. 273, 34575-34579
   Abstract »    Full Text »    PDF »


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