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Science 28 August 1992:
Vol. 257. no. 5074, pp. 1251 - 1255
DOI: 10.1126/science.1519061

Articles

Science, Vol 257, Issue 5074, 1251-1255
Copyright © 1992 by American Association for the Advancement of Science


articles

Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex

WE Meador, AR Means, and FA Quiocho

Howard Hughes Medical Institute, Baylor College of Medicine, Houston, TX 77030.

The crystal structure of calcium-bound calmodulin (Ca(2+)-CaM) bound to a peptide analog of the CaM-binding region of chicken smooth muscle myosin light chain kinase has been determined and refined to a resolution of 2.4 angstroms (A). The structure is compact and has the shape of an ellipsoid (axial ratio approximately 2:1). The bound CaM forms a tunnel diagonal to its long axis that engulfs the helical peptide, with the hydrophobic regions of CaM melded into a single area that closely covers the hydrophobic side of the peptide. There is a remarkably high pseudo-twofold symmetry between the closely associated domains. The central helix of the native CaM is unwound and expanded into a bend between residues 73 and 77. About 185 contacts (less than 4 A) are formed between CaM and the peptide, with van der Waals contacts comprising approximately 80% of this total.


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P. O. Tsvetkov, I. I. Protasevich, R. Gilli, D. Lafitte, V. M. Lobachov, J. Haiech, C. Briand, and A. A. Makarov (1999)
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T. Wagenknecht, M. Radermacher, R. Grassucci, J. Berkowitz, H.-B. Xin, and S. Fleischer (1997)
J. Biol. Chem. 272, 32463-32471
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Characterization of Substrate Phosphorylation and Use of Calmodulin Mutants to Address Implications from the Enzyme Crystal Structure of Calmodulin-dependent Protein Kinase I.
D. Chin, K. E. Winkler, and A. R. Means (1997)
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Brush Border Myosin-I Structure and ADP-dependent Conformational Changes Revealed by Cryoelectron Microscopy and Image Analysis.
J. D. Jontes and R. A. Milligan (1997)
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M. Matsubara, N. Hayashi, K. Titani, and H. Taniguchi (1997)
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The Ca2+-dependent Binding of Calmodulin to an N-terminal Motif of the Heterotrimeric G Protein beta  Subunit.
M. Liu, B. Yu, O. Nakanishi, T. Wieland, and M. Simon (1997)
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S. H. Lee, H. Y. Seo, J. C. Kim, W. D. Heo, W. S. Chung, K. J. Lee, M. C. Kim, Y. H. Cheong, J. Y. Choi, C. O. Lim, et al. (1997)
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D. Chin, D. J. Sloan, F. A. Quiocho, and A. R. Means (1997)
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Kinetic Control of the Dissociation Pathway of Calmodulin-Peptide Complexes.
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   Abstract »    Full Text »    PDF »
Blocking the Ca[IMAGE]-induced Conformational Transitions in Calmodulin with Disulfide Bonds.
R.-Y. Tan, Y. Mabuchi, and Z. Grabarek (1996)
J. Biol. Chem. 271, 7479-7483
   Abstract »    Full Text »    PDF »
Structural Change Mechanisms in Regulatory Proteins.
H. Weinstein and E. L. Mehler (1996)
Science 271, 1792-1793
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Identification, Characterization, and Comparison of the Calmodulin-binding Domains of the Endothelial and Inducible Nitric Oxide Synthases.
R. C. Venema, H. S. Sayegh, J. D. Kent, and D. G. Harrison (1996)
J. Biol. Chem. 271, 6435-6440
   Abstract »    Full Text »    PDF »
Effects of Myosin Light Chain Kinase and Peptides on Ca[IMAGE] Exchange with the N- and C-terminal Ca[IMAGE] Binding Sites of Calmodulin.
J. D. Johnson, C. Snyder, M. Walsh, and M. Flynn (1996)
J. Biol. Chem. 271, 761-767
   Abstract »    Full Text »    PDF »
Covalent Binding of Peptides to the N-terminal Hydrophobic Region of Cardiac Troponin C Has Limited Effects on Function.
X. Lin, D. G. Dotson, and J. A. Putkey (1996)
J. Biol. Chem. 271, 244-249
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The Calmodulin-Nitric Oxide Synthase Interaction.
Z. Su, M. A. Blazing, D. Fan, and S. E. George (1995)
J. Biol. Chem. 270, 29117-29122
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Both the Amino and Carboxyl Termini of Dictyostelium Myosin Essential Light Chain Are Required for Binding to Myosin Heavy Chain.
G. Ho, T.-L. L. Chen, and R. L. Chisholm (1995)
J. Biol. Chem. 270, 27977-27981
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The Regulatory Region of Calcium/Calmodulin-dependent Protein Kinase I Contains Closely Associated Autoinhibitory and Calmodulin-binding Domains.
H. Yokokura, M. R. Picciotto, A. C. Nairn, and H. Hidaka (1995)
J. Biol. Chem. 270, 23851-23859
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Interaction of Calmodulin with Its Binding Domain of Rat Cerebellar Nitric Oxide Synthase.
M. Zhang, T. Yuan, J. M. Aramini, and H. J. Vogel (1995)
J. Biol. Chem. 270, 20901-20907
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Intrasteric Regulation of Myosin Light Chain Kinase.
J. K. Krueger, R. C. Padre, and J. T. Stull (1995)
J. Biol. Chem. 270, 16848-16853
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Calmodulin Binding of a Peptide Derived from the Regulatory Domain of Bordetella pertussis Adenylate Cyclase.
C. T. Craescu, A. Bouhss, J.ël Mispelter, E. Diesis, A. Popescu, M. Chiriac, and O. Bârzu (1995)
J. Biol. Chem. 270, 7088-7096
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Amino-terminal Myristoylation Induces Cooperative Calcium Binding to Recoverin.
J. B. Ames, T. Porumb, T. Tanaka, M. Ikura, and L. Stryer (1995)
J. Biol. Chem. 270, 4526-4533
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The Interaction of Calmodulin with Clathrin-coated Vesicles, Triskelions, and Light Chains.
U. M. Pley, B. L. Hill, C. Alibert, F. M. Brodsky, and P. Parham (1995)
J. Biol. Chem. 270, 2395-2402
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Identification of a Ca(2+)-binding light chain within Chlamydomonas outer arm dynein.
S. King and R. Patel-King (1995)
J. Cell Sci. 108, 3757-3764
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Diverse essential functions revealed by complementing yeast calmodulin mutants.
Y Ohya and D Botstein (1994)
Science 263, 963-966
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Modulation of calmodulin plasticity in molecular recognition on the basis of x-ray structures.
W. Meador, A. Means, and F. Quiocho (1993)
Science 262, 1718-1721
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