Abstract
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 (Å). The structure is compact and has the shape of an ellipsoid (axial ratio ∼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 (<4 Å) are formed between CaM and the peptide, with van der Waals contacts comprising ∼80% of this total.
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Dates
Type | When |
---|---|
Created | 18 years, 10 months ago (Oct. 5, 2006, 7:03 p.m.) |
Deposited | 1 year, 7 months ago (Jan. 11, 2024, 5:24 a.m.) |
Indexed | 2 weeks, 3 days ago (Aug. 5, 2025, 8:44 a.m.) |
Issued | 32 years, 11 months ago (Aug. 28, 1992) |
Published | 32 years, 11 months ago (Aug. 28, 1992) |
Published Print | 32 years, 11 months ago (Aug. 28, 1992) |
@article{Meador_1992, title={Target Enzyme Recognition by Calmodulin: 2.4 Å Structure of a Calmodulin-Peptide Complex}, volume={257}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.1519061}, DOI={10.1126/science.1519061}, number={5074}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Meador, William E. and Means, Anthony R. and Quiocho, Florante A.}, year={1992}, month=aug, pages={1251–1255} }