How do Chaperones Bind (Partly) Unfolded Client Proteins?

ABSTRACT: Molecular chaperones are central to cellular protein homeostasis. Dynamic disorder is a key feature of the complexes of molecular chaperones and their client proteins, and it facilitates the client release towards a folded state or the handover to downstream components. The dynamic nature also implies that a given chaperone can interact with many different client proteins, based on physico-chemical sequence properties rather than on structural complementarity of their (folded) 3D structure. Yet, the balance between this promiscuity and some degree of client specificity is poorly understood. Here, we review recent atomic-level descriptions of chaperones with client proteins, including chaperones in complex with intrinsically disordered proteins, with membrane-protein precursors, or partiall

SUBMITTER: Sucec I 

PROVIDER: S-EPMC8573040 | biostudies-literature | 2021

REPOSITORIES: biostudies-literature