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Article . 1999
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Annual Review of Biochemistry
Article . 1999 . Peer-reviewed
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Annual Review of Biochemistry
Article . 2000
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Annual Review of Biochemistry
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Structural Mechanism of Muscle Contraction

descriptionPublicationkeyboard_double_arrow_right Article 01 Jun 1999Publisher:Annual ReviewsJournal:Annual Review of Biochemistry, volume 68, pages 687-728 (issn: 0066-4154, eissn: 1545-4509, Copyright policy )
Authors: Geeves, M.; Holmes, K.;

doi: 10.1146/annurev.biochem.68.1.687

pmid: 10872464

handle: 11858/00-001M-0000-0024-566B-8 , 11858/00-001M-0000-0024-5669-C

Structural Mechanism of Muscle Contraction

Abstract

▪ 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° to 70° 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.

Related Organizations
Keywords

Sequence Homology, Amino Acid, Molecular Sequence Data, Amino Acid Sequence, Myosins, Actins, Muscle Contraction

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citations
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
697
Top 1%
Top 1%
Top 0.1%
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