Ontology highlight
ABSTRACT:
SUBMITTER: Ryder BD
PROVIDER: S-EPMC7878476 | biostudies-literature | 2021 Feb
REPOSITORIES: biostudies-literature
Ryder Bryan D BD Matlahov Irina I Bali Sofia S Vaquer-Alicea Jaime J van der Wel Patrick C A PCA Joachimiak Lukasz A LA
Nature communications 20210211 1
The Hsp40/Hsp70 chaperone families combine versatile folding capacity with high substrate specificity, which is mainly facilitated by Hsp40s. The structure and function of many Hsp40s remain poorly understood, particularly oligomeric Hsp40s that suppress protein aggregation. Here, we used a combination of biochemical and structural approaches to shed light on the domain interactions of the Hsp40 DnaJB8, and how they may influence recruitment of partner Hsp70s. We identify an interaction between ...[more]