TARGET ENZYME RECOGNITION BY CALMODULIN: 2.4 ANGSTROMS STRUCTURE OF A CALMODULIN-PEPTIDE COMPLEX
[MYLK_CHICK] Phosphorylates a specific serine in the N-terminus of a myosin light chain, which leads to the formation of calmodulin/MLCK signal transduction complexes which allow selective transduction of calcium signals.
Publication Abstract from PubMed
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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.