학술논문
Hsp90 middle domain phosphorylation initiates a complex conformational program to recruit the ATPase-stimulating cochaperone Aha1
Document Type
article
Author
Source
Nature Communications, Vol 10, Iss 1, Pp 1-14 (2019)
Subject
Language
English
ISSN
2041-1723
Abstract
Phosphorylation of Tyr313 in Hsp90 enhances the binding to its activator Aha1, but the underlying mechanism is unknown. Here, the authors study the structural consequences of Tyr313 phosphorylation, showing that it serves as a conformational switch in Hsp90 that enables Aha1 recruitment.