The structure of an Hsp90-immunophilin complex reveals cochaperone recognition of the client maturation state.
Sign Up to like & getrecommendations! Published in 2021 at "Molecular cell"
DOI: 10.1016/j.molcel.2021.07.023
Abstract: The Hsp90 chaperone promotes folding and activation of hundreds of client proteins in the cell through an ATP-dependent conformational cycle guided by distinct cochaperone regulators. The FKBP51 immunophilin binds Hsp90 with its tetratricopeptide repeat (TPR)… read more here.
Keywords: hsp90; client; cochaperone; client maturation ... See more keywords