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Title: Myosin cleft movement and its coupling to actomyosin dissociation
Authors: Conibear, Paul B.
Bagshaw, Clive R.
Fajer, Piotr G.
Kovács, Mihály
Málnási-Csizmadia, András
First Published: Oct-2003
Publisher: Nature Publishing Group
Citation: Nature Structural and Molecular Biology, 2003, 10(10), pp. 831-835
Abstract: It has long been known that binding of actin and nucleotides to myosin are antagonistic, an observation that led to the biochemical basis for the crossbridge cycle of muscle contraction. Thus ATP binding to actomyosin causes actin dissociation, while actin binding to the myosin accelerates ADP and phosphate release. Structural studies have indicated that communication between the actin and nucleotide binding sites involves the opening and closing of the cleft between the upper and lower 50K domains of the myosin he ad. Here we test the proposal that the cleft responds to actin and nucleotide binding in a reciprocal manner and show that cleft movement is coupled to actin binding and dissociation. We monitored cleft movement using pyrene excimer fluorescence from probes engineered across the cleft.
DOI Link: 10.1038/nsb986
ISSN: 1545-9993
eISSN: 1545-9985
Version: Post print
Status: Peer reviewed
Type: Article
Rights: Copyright 2003 Nature Publishing Group. Deposited with reference to the publisher's archiving policy available on the SHERPA/RoMEO website.
Description: This is the authors' final draft of a paper published as Nature Structural Biology, 2003, 10(10), pp.773-775
Appears in Collections:Published Articles, Dept. of Biochemistry

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