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PMID: 16563742 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Review

Structure and function of myosin filaments.

Current opinion in structural biology ·Vol. 16 ·No. 2 ·2006-04-00 ·Pages 204-12

Craig R, Woodhead JL

Abstract

Myosin filaments interact with actin to generate muscle contraction and many forms of cell motility. X-ray and electron microscopy (EM) studies have revealed the general organization of myosin molecules in relaxed filaments, but technical difficulties have prevented a detailed description. Recent studies using improved ultrastructural and image analysis techniques are overcoming these problems. Three-dimensional reconstructions using single-particle methods have provided many new insights into the organization of the myosin heads and tails. Docking of atomic structures into cryo-EM density maps suggests how regulated myosin filaments are 'switched off', bringing about muscle relaxation. Additionally, sequence analysis suggests probable interactions between myosin tails in the backbone, whereas crystallographic and EM studies are starting to reveal tail interactions directly in three dimensions.

MeSH Terms
Actin Cytoskeleton/physiology,ultrastructure Animals Models, Biological Muscle Contraction Muscle, Skeletal/physiology,ultrastructure Muscle, Smooth/physiology,ultrastructure Myosin Subfragments/physiology,ultrastructure Myosins/physiology,ultrastructure
Chemicals
Myosin Subfragments Myosins
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Craig Roger
Department of Cell Biology, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, MA 01655, USA. [email protected]
Woodhead John L
Article Info
Journal
Current opinion in structural biology
Abbr.
Curr Opin Struct Biol
ISSN
0959-440X
Published
2006-04-00
Epub
2006-00-24
Pages
204-12
Language
English
Region
England
NLM ID
9107784
Subset
IM
Grants
NIAMS NIH HHS · R01 AR034711 · United States
NIAMS NIH HHS · AR34711 · United States
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