Ontology highlight
ABSTRACT:
SUBMITTER: Xu W
PROVIDER: S-EPMC6561935 | biostudies-literature | 2019 Jun
REPOSITORIES: biostudies-literature
Xu Wanping W Beebe Kristin K Chavez Juan D JD Boysen Marta M Lu YinYing Y Zuehlke Abbey D AD Keramisanou Dimitra D Trepel Jane B JB Prodromou Christosomos C Mayer Matthias P MP Bruce James E JE Gelis Ioannis I Neckers Len L
Nature communications 20190612 1
Complex conformational dynamics are essential for function of the dimeric molecular chaperone heat shock protein 90 (Hsp90), including transient, ATP-biased N-domain dimerization that is necessary to attain ATPase competence. The intrinsic, but weak, ATP hydrolyzing activity of human Hsp90 is markedly enhanced by the co-chaperone Aha1. However, the cellular concentration of Aha1 is substoichiometric relative to Hsp90. Here we report that initial recruitment of this cochaperone to Hsp90 is marked ...[more]