ATPase subdomain IA is a mediator of interdomain allostery in Hsp70 molecular chaperones.

ABSTRACT: The versatile functions of the heat shock protein 70 (Hsp70) family of molecular chaperones rely on allosteric interactions between their nucleotide-binding and substrate-binding domains, NBD and SBD. Understanding the mechanism of interdomain allostery is essential to rational design of Hsp70 modulators. Yet, despite significant progress in recent years, how the two Hsp70 domains regulate each other's activity remains elusive. Covariance data from experiments and computations emerged in recent years as valuable sources of information towards gaining insights into the molecular events that mediate allostery. In the present study, conservation and covariance properties derived from both sequence and structural dynamics data are integrated with results from Perturbation Response Scanning and

SUBMITTER: General IJ 

PROVIDER: S-EPMC4022485 | biostudies-literature | 2014 May

REPOSITORIES: biostudies-literature