Journal
BIOCHEMISTRY
Volume 48, Issue 12, Pages 2710-2713Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi900223x
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- Muscular Dystrophy Association
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The dynein motor proteins interact with microtubules at the distal end of an unusual 12-15 nm stalk, which communicates with the sites for nucleotide hydrolysis and microtubule binding in a cyclical, bidirectional manner. Here, we report that the stalk shaft of rat cytoplasmic dynein is an antiparallel a-helical coiled coil, the stability of which is markedly altered by changes at its proximal and distal ends, consistent with a structure capable of rapid, cyclical rearrangement during the dynein cross-bridge cycle.
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