1mux

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SOLUTION NMR STRUCTURE OF CALMODULIN/W-7 COMPLEX: THE BASIS OF DIVERSITY IN MOLECULAR RECOGNITION, 30 STRUCTURES

Overview

The solution structure of calcium-bound calmodulin (CaM) complexed with an, antagonist, N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide (W-7), has, been determined by multidimensional NMR spectroscopy. The structure, consists of one molecule of W-7 binding to each of the two domains of CaM., In each domain, the W-7 chloronaphthalene ring interacts with four, methionine methyl groups and other aliphatic or aromatic side-chains in a, deep hydrophobic pocket, the site responsible for CaM binding to, CaM-dependent enzymes such as myosin light chain kinases (MLCKs) and CaM, kinase II. This competitive binding at the same site between W-7 and, CaM-dependent enzymes suggests the mechanism by which W-7 inhibits CaM to, activate the enzymes. The orientation of the W-7 naphthalene ring in the, N-terminal pocket is rotated approximately 40 degrees with respect to that, in the C-terminal pocket. The W-7 ring orientation differs significantly, from the Trp800 indole ring of smooth muscle MLCK bound to the C-terminal, pocket and the phenothiazine ring of trifluoperazine bound to the N or, C-terminal pocket. These comparative structural analyses demonstrate that, the two hydrophobic pockets of CaM can accommodate a variety of bulky, aromatic rings, which provides a plausible structural basis for the, diversity in CaM-mediated molecular recognition.

About this Structure

1MUX is a Single protein structure of sequence from Xenopus laevis with CA and WW7 as ligands. Full crystallographic information is available from OCA.

Reference

Solution structure of calmodulin-W-7 complex: the basis of diversity in molecular recognition., Osawa M, Swindells MB, Tanikawa J, Tanaka T, Mase T, Furuya T, Ikura M, J Mol Biol. 1998 Feb 13;276(1):165-76. PMID:9514729

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