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- W1981256246 abstract "Abstract The structures of the complexes between calcium-bound calmodulin and synthetic peptides comprising the calmodulin-binding domain of skeletal and smooth muscle myosin light-chain kinase have now been solved by NMR and X-ray crystallography, respectively. Within coordinate errors, there are no significant differences between the two structures. The two domains of calmodulin (residues 6–73 and 83–146) remain essentially unchanged upon complexation. The long central helix (residues 65–93) which connects the two domains in the crystal structure of calcium-bound calmodulin, however, is disrupted in the complex into two helices connected by a long flexible loop (residues 74–82), thereby enabling the two domains to clamp the bound peptide which adopts a helical conformation. The overall structure of the complex is globular, approximating an ellipsoid of dimensions 47 × 32 × 30 A . The helical peptide is located in a hydrophobic channel which passes through the center of the ellipsoid at an angle of 45° to its long axis." @default.
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- W1981256246 date "1993-01-01" @default.
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- W1981256246 title "Structure of calmodulin-target peptide complexes" @default.
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- W1981256246 doi "https://doi.org/10.1016/0959-440x(93)90146-c" @default.
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