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Science 1 May 1992:
Vol. 256. no. 5057, pp. 632 - 638
DOI: 10.1126/science.1585175
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Articles

Science, Vol 256, Issue 5057, 632-638
Copyright © 1992 by American Association for the Advancement of Science

articles

Solution structure of a calmodulin-target peptide complex by multidimensional NMR

M Ikura, GM Clore, AM Gronenborn, G Zhu, CB Klee, and A Bax

Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.

The three-dimensional solution structure of the complex between calcium-bound calmodulin (Ca(2+)-CaM) and a 26-residue synthetic peptide comprising the CaM binding domain (residues 577 to 602) of skeletal muscle myosin light chain kinase, has been determined using multidimensional heteronuclear filtered and separated nuclear magnetic resonance spectroscopy. The two domains of CaM (residues 6 to 73 and 83 to 146) remain essentially unchanged upon complexation. The long central helix (residues 65 to 93), however, which connects the two domains in the crystal structure of Ca(2+)-CaM, is disrupted into two helices connected by a long flexible loop (residues 74 to 82), thereby enabling the two domains to clamp residues 3 to 21 of the bound peptide, which adopt a helical conformation. The overall structure of the complex is globular, approximating an ellipsoid of dimensions 47 by 32 by 30 angstroms. The helical peptide is located in a hydrophobic channel that passes through the center of the ellipsoid at an angle of approximately 45 degrees with its long axis. The complex is mainly stabilized by hydrophobic interactions which, from the CaM side, involve an unusually large number of methionines. Key residues of the peptide are Trp4 and Phe17, which serve to anchor the amino- and carboxyl-terminal halves of the peptide to the carboxyl- and amino-terminal domains of CaM, respectively. Sequence comparisons indicate that a number of peptides that bind CaM with high affinity share this common feature containing either aromatic residues or long-chain hydrophobic ones separated by a stretch of 12 residues, suggesting that they interact with CaM in a similar manner.


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J. Biol. Chem. 273, 9148-9157
   Abstract »    Full Text »    PDF »
Regulation of Calcyclin (S100A6) Binding by Alternative Splicing in the N-terminal Regulatory Domain of Annexin XI Isoforms.
T. Sudo and H. Hidaka (1998)
J. Biol. Chem. 273, 6351-6357
   Abstract »    Full Text »    PDF »
Signaling pathways underlying eosinophil cell motility revealed by using caged peptides.
J. W. Walker, S. H. Gilbert, R. M. Drummond, M. Yamada, R. Sreekumar, R. E. Carraway, M. Ikebe, and F. S. Fay (1998)
PNAS 95, 1568-1573
   Abstract »    Full Text »    PDF »
Specificity and Symmetry in the Interaction of Calmodulin Domains with the Skeletal Muscle Myosin Light Chain Kinase Target Sequence.
A. Barth, S. R. Martin, and P. M. Bayley (1998)
J. Biol. Chem. 273, 2174-2183
   Abstract »    Full Text »    PDF »
Locations of Calmodulin and FK506-binding Protein on the Three-dimensional Architecture of the Skeletal Muscle Ryanodine Receptor.
T. Wagenknecht, M. Radermacher, R. Grassucci, J. Berkowitz, H.-B. Xin, and S. Fleischer (1997)
J. Biol. Chem. 272, 32463-32471
   Abstract »    Full Text »    PDF »
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)
J. Biol. Chem. 272, 31235-31240
   Abstract »    Full Text »    PDF »
Interaction of the Second Binding Region of Troponin I with the Regulatory Domain of Skeletal Muscle Troponin C as Determined by NMR Spectroscopy.
R. T. McKay, B. P. Tripet, R. S. Hodges, and B. D. Sykes (1997)
J. Biol. Chem. 272, 28494-28500
   Abstract »    Full Text »    PDF »
Circular Dichroism and 1H NMR Studies on the Structures of Peptides Derived from the Calmodulin-binding Domains of Inducible and Endothelial Nitric-oxide Synthase in Solution and in Complex with Calmodulin. NASCENT alpha -HELICAL STRUCTURES ARE STABILIZED BY CALMODULIN BOTH IN THE PRESENCE AND ABSENCE OF Ca2+.
M. Matsubara, N. Hayashi, K. Titani, and H. Taniguchi (1997)
J. Biol. Chem. 272, 23050-23056
   Abstract »    Full Text »    PDF »
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)
J. Biol. Chem. 272, 18801-18807
   Abstract »    Full Text »    PDF »
Structure of Cardiac Muscle Troponin C Unexpectedly Reveals a Closed Regulatory Domain.
S. K. Sia, M. X. Li, L. Spyracopoulos, S. M. Gagne, W. Liu, J. A. Putkey, and B. D. Sykes (1997)
J. Biol. Chem. 272, 18216-18221
   Abstract »    Full Text »    PDF »
Identification and Characterization of a Calmodulin-binding Domain in Ral-A, a Ras-related GTP-binding Protein Purified from Human Erythrocyte Membrane.
K. L. Wang, M. T. Khan, and B. D. Roufogalis (1997)
J. Biol. Chem. 272, 16002-16009
   Abstract »    Full Text »    PDF »
Differential Activation of NAD Kinase by Plant Calmodulin Isoforms. THE CRITICAL ROLE OF DOMAIN I.
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)
J. Biol. Chem. 272, 9252-9259
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Circular Dichroism and 1H Nuclear Magnetic Resonance Studies on the Solution and Membrane Structures of GAP-43 Calmodulin-binding Domain.
N. Hayashi, M. Matsubara, K. Titani, and H. Taniguchi (1997)
J. Biol. Chem. 272, 7639-7645
   Abstract »    Full Text »    PDF »
Functional Consequences of Truncating Amino Acid Side Chains Located at a Calmodulin-Peptide Interface.
D. Chin, D. J. Sloan, F. A. Quiocho, and A. R. Means (1997)
J. Biol. Chem. 272, 5510-5513
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Kinetic Control of the Dissociation Pathway of Calmodulin-Peptide Complexes.
S. E. Brown, S. R. Martin, and P. M. Bayley (1997)
J. Biol. Chem. 272, 3389-3397
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Localization of Unique Functional Determinants in the Calmodulin Lobes to Individual EF Hands.
A. Persechini, P. M. Stemmer, and I. Ohashi (1996)
J. Biol. Chem. 271, 32217-32225
   Abstract »    Full Text »    PDF »


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