A second tubulin binding site on the kinesin-13 motor head domain is important during mitosis.
Kinesin-13s are microtubule (MT) depolymerases different from most other kinesins that move along MTs. Like other kinesins, they have a motor or head domain (HD) containing a tubulin and an ATP binding site. Interestingly, kinesin-13s have an additional binding site (Kin-Tub-2) on the opposite side...
Saved in:
Main Authors: | Dong Zhang, Ana B Asenjo, Michaela Greenbaum, Luping Xie, David J Sharp, Hernando Sosa |
---|---|
Format: | article |
Language: | EN |
Published: |
Public Library of Science (PLoS)
2013
|
Subjects: | |
Online Access: | https://doaj.org/article/3a2e77f84f824dfabd3fd7f6445f5e4b |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
Cryo-EM reveals the structural basis of microtubule depolymerization by kinesin-13s
by: Matthieu P.M.H. Benoit, et al.
Published: (2018) -
Author Correction: Cryo-EM reveals the structural basis of microtubule depolymerization by kinesin-13s
by: Matthieu P. M. H. Benoit, et al.
Published: (2018) -
Insight into microtubule disassembly by kinesin-13s from the structure of Kif2C bound to tubulin
by: Weiyi Wang, et al.
Published: (2017) -
Ternary complex of Kif2A-bound tandem tubulin heterodimers represents a kinesin-13-mediated microtubule depolymerization reaction intermediate
by: Daria Trofimova, et al.
Published: (2018) -
Structural basis of mechano-chemical coupling by the mitotic kinesin KIF14
by: Matthieu P.M.H. Benoit, et al.
Published: (2021)