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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5821
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pubmed:dateCreated |
1981-9-15
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pubmed:abstractText |
The topography of the rigor complex between F-actin and myosin heads (S1) has been investigated by carbodiimide zero-length cross-linking. The results demonstrate for the first time that the 95,000-molecular weight (95K) heavy chain of the myosin head enters into van der Waals contact with two neighbouring actin monomers; one is bound to the 50K domain and the other to the 20K domain of the myosin chain. The covalent F-actin-S1 complex can be isolated; it shows a vastly elevated Mg2+-ATPase. Each pair of actin subunits in the thin filament seems to act as a functional unit for specific binding of a myosin head and stimulation of its Mg2+-ATPase activity.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0028-0836
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
292
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
301-6
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:6114435-Actins,
pubmed-meshheading:6114435-Actomyosin,
pubmed-meshheading:6114435-Adenosine Triphosphatases,
pubmed-meshheading:6114435-Animals,
pubmed-meshheading:6114435-Binding Sites,
pubmed-meshheading:6114435-Ca(2+) Mg(2+)-ATPase,
pubmed-meshheading:6114435-Kinetics,
pubmed-meshheading:6114435-Macromolecular Substances,
pubmed-meshheading:6114435-Molecular Weight,
pubmed-meshheading:6114435-Myosins,
pubmed-meshheading:6114435-Protein Binding,
pubmed-meshheading:6114435-Protein Conformation
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pubmed:year |
1981
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pubmed:articleTitle |
Structure of the actin-myosin interface.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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