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PubMed · 2958487

Dynein structure and function.

K A Johnson·S P Marchese-Ragona·D B Clutter·E L Holzbaur·T J Chilcote
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Abstract

The structure of dynein isolated from several sources follows the pattern first observed with Tetrahymena 22S dynein, which has three globular heads attached by three flexible strands to a root-like base. Recent biochemical data indicate that there is one ATPase site on each dynein head and that all three heads interact with microtubules in an ATP-sensitive manner. Accordingly, images of dynein in situ can be interpreted in terms of a model for crossbridge action where the roots of the bouquet anchor the dynein to the A-tubule and all three heads reach out to interact with the B-tubule in an ATP-dependent reaction to produce a force for sliding.

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Adenosine TriphosphatasesAdenosine TriphosphateAnimalsBinding SitesDyneinsMicrotubulesModels, BiologicalStructure-Activity RelationshipJournal ArticleResearch Support, Non-U.S. Gov'tResearch Support, U.S. Gov't, P.H.S.Review

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K A Johnson, S P Marchese-Ragona, D B Clutter, E L Holzbaur, T J Chilcote. 1986. Dynein structure and function.. https://doi.org/10.1242/jcs.1986.supplement_5.12

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