1cdl
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(New page: 200px<br /> <applet load="1cdl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cdl, resolution 2.0Å" /> '''TARGET ENZYME RECOGN...)
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Revision as of 14:14, 12 November 2007
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TARGET ENZYME RECOGNITION BY CALMODULIN: 2.4 ANGSTROMS STRUCTURE OF A CALMODULIN-PEPTIDE COMPLEX
Contents |
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.
Disease
Known diseases associated with this structure: Cavernous malformations of CNS and retina OMIM:[604214], Cerebral cavernous malformations-1 OMIM:[604214], Hyperkeratotic cutaneous capillary-venous malformations associated with cerebral capillary malformations OMIM:[604214], Leukemia, acute T-cell lymphoblastic OMIM:[603025], Leukemia, acute myeloid OMIM:[603025]
About this Structure
1CDL is a Protein complex structure of sequences from Homo sapiens with CA as ligand. 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
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