Open AccessTarget sequence recognition by the calmodulin superfamily: implications from light chain binding to the regulatory domain of scallop myosin.
Author(s) -
Anne Houdusse,
Carolyn Cohen
Publication year - 1995
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.92.23.10644
Subject(s) - calmodulin , myosin , ef hand , scallop , myosin light chain kinase , superfamily , immunoglobulin light chain , biology , phd finger , protein structure , sequence alignment , computational biology , peptide sequence , calcium binding protein , biochemistry , gene , genetics , chemistry , calcium , zinc finger , transcription factor , ecology , enzyme , organic chemistry , antibody
Some of the rules for how members of the calmodulin (CaM) superfamily bind to target peptides are revealed by the crystal structure of the regulatory domain of scallop myosin. The structure shows that the IQ motif of the heavy chain in this invertebrate myosin imposes constraints on both the positioning and conformation of the individual lobes of the light chains. In contrast, analysis of the contact residues in the targets bound by Ca(2+)-CaM reveals how the structure of CaM accommodates a broader range of sequences consonant with this protein's functional diversity.