Structural Basis for Protein Folding and Holding Mediated by Molecular Chaperones

Abstract

During protein synthesis, folding, and translocation, proteins called molecular chaperones play key roles through the mechanisms that are not well understood. The scarcity of the high-resolution structural information for the interaction between chaperones and the client proteins, which are typically in an unfolded state, had prevented the elucidation of the detailed mechanisms. However, recent NMR studies have determined several key structures of chaperones in complex with client proteins. Here in this review, we summarize the recent structural studies on molecular chaperones that shed light on how the chaperones regulate the folding and translocation of the client proteins.