Ontology highlight
ABSTRACT:
SUBMITTER: Burns KM
PROVIDER: S-EPMC4386277 | biostudies-literature | 2014 Aug
REPOSITORIES: biostudies-literature
Burns Kyle M KM Wagenbach Mike M Wordeman Linda L Schriemer David C DC
Structure (London, England : 1993) 20140724 8
Members of the kinesin-13 subfamily use motor domains in an unconventional fashion to initiate microtubule (MT) depolymerization at MT ends, suggesting unique conformational transitions for lattice engagement, end adaptation, or both. Using hydrogen-deuterium exchange and electron microscopy, we explored conformational changes in free dimeric mitotic centromere-associated kinesin (MCAK) and when bound to a depolymerization intermediate. ATP hydrolysis relaxes the conformation of the dimer, notab ...[more]