Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex.


Journal Article

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.

Full Text

Duke Authors

Cited Authors

  • Meador, WE; Means, AR; Quiocho, FA

Published Date

  • August 28, 1992

Published In

Volume / Issue

  • 257 / 5074

Start / End Page

  • 1251 - 1255

PubMed ID

  • 1519061

Pubmed Central ID

  • 1519061

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.1519061


  • eng

Conference Location

  • United States