Structural mechanism of muscle contraction

Geeves, M.A. and Holmes, K.C. (1999) Structural mechanism of muscle contraction. Review of: Structural mechanism of muscle contraction by UNSPECIFIED. Annual Review of Biochemistry, 68 . pp. 687-728. ISSN 0066-4154. (The full text of this publication is not available from this repository)

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Official URL
http://dx.doi.org/10.1146/annurev.biochem.68.1.687

Abstract

X-ray crystallography shows the myosin cross-bridge to exist in two conformations, the beginning and end of the "power stroke." A long lever-arm undergoes a 60 degrees to 70 degrees rotation between the two states. This rotation is coupled with changes in the active site (OPEN to CLOSED) and phosphate release. Actin binding mediates the transition from CLOSED to OPEN. Kinetics shows that the binding of myosin to actin is a two-step process which affects ATP and ADP affinity. The structural basis of these effects is not explained by the presently known conformers of myosin. Therefore, other states of the myosin cross-bridge must exist. Moreover, cryoelectronmicroscopy has revealed other angles of the cross-bridge lever arm induced by ADP binding. These structural states are presently being characterized by site-directed mutagenesis coupled with kinetic analysis.

Item Type: Review
Uncontrolled keywords: actin; myosin; structure; muscle contraction; swinging cross bridge; molecular mechanism; kinetics; mutations
Subjects: Q Science
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: I.T. Ekpo
Date Deposited: 29 Apr 2009 22:23
Last Modified: 29 Apr 2009 22:23
Resource URI: http://kar.kent.ac.uk/id/eprint/16802 (The current URI for this page, for reference purposes)
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