1cdl
From Proteopedia
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'''TARGET ENZYME RECOGNITION BY CALMODULIN: 2.4 ANGSTROMS STRUCTURE OF A CALMODULIN-PEPTIDE COMPLEX''' | '''TARGET ENZYME RECOGNITION BY CALMODULIN: 2.4 ANGSTROMS STRUCTURE OF A CALMODULIN-PEPTIDE COMPLEX''' | ||
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[[Category: Meador, W E.]] | [[Category: Meador, W E.]] | ||
[[Category: Quiocho, F A.]] | [[Category: Quiocho, F A.]] | ||
| - | [[Category: | + | [[Category: Calcium-binding protein]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:36:44 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 09:36, 2 May 2008
TARGET ENZYME RECOGNITION BY CALMODULIN: 2.4 ANGSTROMS STRUCTURE OF A CALMODULIN-PEPTIDE COMPLEX
Overview
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.
About this Structure
1CDL is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex., Meador WE, Means AR, Quiocho FA, Science. 1992 Aug 28;257(5074):1251-5. PMID:1519061 Page seeded by OCA on Fri May 2 12:36:44 2008
