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PMID: 4039721 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Three-dimensional image analysis of the complex of thin filaments and myosin molecules from skeletal muscle. V. Assignment of actin in the actin-tropomyosin-myosin subfragment-1 complex.

Journal of biochemistry ·Vol. 97 ·No. 1 ·1985-01-00 ·Pages 245-63

Toyoshima C, Wakabayashi T

Abstract

To assign the actin molecule in the three-dimensional image of the actin-tropomyosin-myosin subfragment-1 (actin-TM-S1) complex, the three-dimensional image of the actin-tropomyosin complex was correlated to that of actin-TM-S1. To assess the similarity of two structures in a quantitative manner, we used a normalized cross-correlation function ("similarity function"). The calculation of similarity indicated that domain A and domain B defined in (1, 2) correspond to actin-tropomyosin. This assignment indicates that one S1 molecule strongly interacts with only one actin molecule, but at least two regions of S1 contribute to the binding. Comparison of the reconstituted models of thin filaments with those of decorated thin filaments suggested a change in the shape of the actin molecule.

MeSH Terms
Actins Animals Chemical Phenomena Chemistry, Physical Cytoskeleton/ultrastructure Macromolecular Substances Microscopy, Electron Models, Molecular Muscles/ultrastructure Myosin Subfragments Myosins Peptide Fragments Protein Conformation Rabbits Tropomyosin
Chemicals
Actins Macromolecular Substances Myosin Subfragments Peptide Fragments Tropomyosin Myosins
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Toyoshima C
Wakabayashi T
Article Info
Journal
Journal of biochemistry
Abbr.
J Biochem
ISSN
0021-924X
Published
1985-01-00
Pages
245-63
Language
English
Region
England
NLM ID
0376600
Subset
IM
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