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Reference: Ogura K, et al. (2012) Conformational dynamics of yeast calmodulin in the Ca(2+)-bound state probed using NMR relaxation dispersion. FEBS Lett 586(16):2548-54

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Abstract


Most calmodulin (CaM) in apo and Ca(2+)-bound states show a dumb-bell-like structure, involving the N- and C-terminal domains, connected with a flexible linker. However, Ca(2+)-bound yeast calmodulin (yCaM) takes on a unique globular structure; the target-binding site of this protein is autoinhibited. We applied NMR relaxation dispersion experiments to yCaM in the Ca(2+)-bound state. The amide (15)N and (1)H(N) relaxation dispersion profiles indicated the presence of conformational dynamics for specific residues at the interface between the N- and C-terminal domains. We conclude that these conformational dynamics were derived from the mobility of the C-terminal domain.

Reference Type
Journal Article
Authors
Ogura K, Okamura H, Katahira M, Katoh E, Inagaki F
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