| Literature DB >> 2958487 |
K A Johnson1, S P Marchese-Ragona, D B Clutter, E L Holzbaur, T J Chilcote.
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.Entities:
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Year: 1986 PMID: 2958487 DOI: 10.1242/jcs.1986.supplement_5.12
Source DB: PubMed Journal: J Cell Sci Suppl ISSN: 0269-3518