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PMID: 8127365 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Structure of the regulatory domain of scallop myosin at 2.8 A resolution.

Nature ·Vol. 368 ·No. 6469 ·1994-03-24 ·Pages 306-12

Xie X, Harrison DH, Schlichting I, Sweet RM, Kalabokis VN, Szent-Györgyi AG, Cohen C

Abstract

The regulatory domain of scallop myosin is a three-chain protein complex that switches on this motor in response to Ca2+ binding. This domain has been crystallized and the structure solved to 2.8 A resolution. Side-chain interactions link the two light chains in tandem to adjacent segments of the heavy chain bearing the IQ-sequence motif. The Ca(2+)-binding site is a novel EF-hand motif on the essential light chain and is stabilized by linkages involving the heavy chain and both light chains, accounting for the requirement of all three chains for Ca2+ binding and regulation in the intact myosin molecule.

MeSH Terms
Amino Acid Sequence Animals Binding Sites Calcium/metabolism Computer Graphics Crystallography, X-Ray Molecular Sequence Data Mollusca Myosins/chemistry,metabolism,physiology Peptide Fragments/chemistry,metabolism Protein Conformation
Chemicals
Peptide Fragments Myosins Calcium
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Xie X
Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, Massachusetts 02254-9110.
Harrison D H
Schlichting I
Sweet R M
Kalabokis V N
Szent-Györgyi A G
Cohen C
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1994-03-24
Pages
306-12
Language
English
Region
England
NLM ID
0410462
Subset
IM
Corrections
CommentIn
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