The dynein stalk contains an antiparallel coiled coil with region-specific stability.
Biochemistry
; 48(12): 2710-3, 2009 Mar 31.
Article
em En
| MEDLINE
| ID: mdl-19222235
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.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Dineínas
Limite:
Animals
Idioma:
En
Ano de publicação:
2009
Tipo de documento:
Article