钙调蛋白
酶
肽
化学
生物化学
计算生物学
生物
作者
William E. Meador,Anthony R. Means,Florante A. Quiocho
出处
期刊:Science
[American Association for the Advancement of Science]
日期:1992-08-28
卷期号:257 (5074): 1251-1255
被引量:1033
标识
DOI:10.1126/science.1519061
摘要
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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