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Molecular mechanism of actomyosin-based motility

Geeves, Michael A., Fedorov, Roman, Manstein, Dietmar J. (2005) Molecular mechanism of actomyosin-based motility. Cellular and Molecular Life Sciences, 62 (13). pp. 1462-77. ISSN 1420-682X. (doi:10.1007/s00018-005-5015-5) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:13206)

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Sophisticated molecular genetic, biochemical and biophysical studies have been used to probe the molecular mechanism of actomyosin-based motility. Recent solution measurements, high-resolution structures of recombinant myosin motor domains, and lower resolution structures of the complex formed by filamentous actin and the myosin motor domain provide detailed insights into the mechanism of chemomechanical coupling in the actomyosin system. They show how small conformational changes are amplified by a lever-arm mechanism to a working stroke of several nanometres, explain the mechanism that governs the directionality of actin-based movement, and reveal a communication pathway between the nucleotide binding pocket and the actin-binding region that explains the reciprocal relationship between actin and nucleotide affinity. Here we focus on the interacting elements in the actomyosin system and the communication pathways in the myosin motor domain that respond to actin binding.

Item Type: Article
DOI/Identification number: 10.1007/s00018-005-5015-5
Additional information: 1420-682X (Print) Journal Article Review
Uncontrolled keywords: Actins/chemistry/metabolism Actomyosin/chemistry/metabolism/*physiology Animals Humans Molecular Motors Movement/*physiology Myosins/chemistry/metabolism Protein Binding Protein Structure, Tertiary Recombinant Proteins Research Support, Non-U.S. Gov't
Subjects: Q Science
Divisions: Divisions > Division of Natural Sciences > Biosciences
Depositing User: Michael Geeves
Date Deposited: 04 Apr 2009 19:13 UTC
Last Modified: 16 Nov 2021 09:51 UTC
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