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PMID: 8316858 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 actin-myosin complex and its implications for muscle contraction.

Science (New York, N.Y.) ·Vol. 261 ·No. 5117 ·1993-07-02 ·Pages 58-65

Rayment I, Holden HM, Whittaker M, Yohn CB, Lorenz M, Holmes KC, Milligan RA

Abstract

Muscle contraction consists of a cyclical interaction between myosin and actin driven by the concomitant hydrolysis of adenosine triphosphate (ATP). A model for the rigor complex of F actin and the myosin head was obtained by combining the molecular structures of the individual proteins with the low-resolution electron density maps of the complex derived by cryo-electron microscopy and image analysis. The spatial relation between the ATP binding pocket on myosin and the major contact area on actin suggests a working hypothesis for the crossbridge cycle that is consistent with previous independent structural and biochemical studies.

MeSH Terms
Actins/chemistry,metabolism Actomyosin/chemistry,metabolism Adenosine Triphosphate/metabolism Binding Sites Image Processing, Computer-Assisted Models, Molecular Muscle Contraction Myosin Subfragments/chemistry,metabolism Protein Conformation Protein Structure, Secondary X-Ray Diffraction
Chemicals
Actins Myosin Subfragments Adenosine Triphosphate Actomyosin
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Rayment I
Department of Biochemistry, University of Wisconsin, Madison 53705.
Holden H M
Whittaker M
Yohn C B
Lorenz M
Holmes K C
Milligan R A
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
1993-07-02
Pages
58-65
Language
English
Region
United States
NLM ID
0404511
Subset
IM
Corrections
CommentIn
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