The dynein stalk contains an antiparallel coiled coil with region-specific stability

Biochemistry. 2009 Mar 31;48(12):2710-3. doi: 10.1021/bi900223x.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Dyneins / chemistry*
  • Dyneins / metabolism
  • Microtubule-Associated Proteins / chemistry
  • Microtubule-Associated Proteins / metabolism
  • Models, Molecular
  • Mutagenesis, Site-Directed
  • Protein Conformation
  • Rats

Substances

  • Microtubule-Associated Proteins
  • Dyneins