The dynein stalk contains an antiparallel coiled coil with region-specific stability.
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 alpha-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.
Höök
Peter
P
Department of Pathology and Cell Biology, Columbia University, New York, New York 10032, USA.
Yagi
Toshiki
T
Ghosh-Roy
Anindya
A
Williams
John C
JC
Vallee
Richard B
RB
D000818:Animals; D004398:Dyneins / Q000737:chemistry* / Q000378:metabolism; D008869:Microtubule-Associated Proteins / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D011487:Protein Conformation; D051381:Rats
D008869:Microtubule-Associated Proteins; D004398:Dyneins