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J Struct Biol. 2006 Oct;156(1):175-81. Epub 2006 Mar 29.

Autoinhibitory and other autoregulatory elements within the dynein motor domain.

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  • 1Department of Pathology and Cell Biology, Columbia University College of Physicians and Surgeons, P and S 15-410, 630 W. 168th St., New York, NY 10032, USA.


The dyneins are a family of microtubule motor proteins. The motor domain, which represents the C-terminal 2/3 of the dynein heavy chain, exhibits homology to the AAA family of ATPases. It consists of a ring of six related but divergent AAA+ units, with two substantial sized protruding projections, the stem, or tail, which anchors the protein to diverse subcellular sites, and the stalk, which binds microtubules. This article reviews recent efforts to probe the mechanism by which the dyneins produce force, and work from the authors' lab regarding long-range conformational regulation of dynein enzymatic activity.

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