Computationally-Aided Modeling of Hsp70-Client Interactions: Past, Present, and Future.

ABSTRACT: Hsp70 molecular chaperones play central roles in maintaining a healthy cellular proteome. Hsp70s function by binding to short peptide sequences in incompletely folded client proteins, thus preventing them from misfolding and/or aggregating, and in many cases holding them in a state that is competent for subsequent processes like translocation across membranes. There is considerable interest in predicting the sites where Hsp70s may bind their clients, as the ability to do so sheds light on the cellular functions of the chaperone. In addition, the capacity of the Hsp70 chaperone family to bind to a broad array of clients and to identify accessible sequences that enable discrimination of those that are folded from those that are not fully folded, which is essential to their cellular roles, is

SUBMITTER: Nordquist EB 

PROVIDER: S-EPMC10309085 | biostudies-literature | 2022 Sep

REPOSITORIES: biostudies-literature