Structural and biochemical insights into FKBP51 as a Hsp90 co‐chaperone

Author:

Baischew Asat1ORCID,Engel Sarah1ORCID,Geiger Thomas M.1ORCID,Taubert Martha C.1,Hausch Felix1ORCID

Affiliation:

1. Department of Chemistry, Institute for Organic Chemistry and Biochemistry Technical University Darmstadt Darmstadt Germany

Abstract

AbstractThe FK506‐binding protein 51 (FKBP51) is a high‐molecular‐weight immunophilin that emerged as an important drug target for stress‐related disorders, chronic pain, and obesity. It has been implicated in a plethora of molecular pathways but remains best characterized as a co‐chaperone of Hsp90 in the steroid hormone receptor (SHR) maturation cycle. However, the mechanistic and structural basis for the regulation of SHRs by FKBP51 and the usually antagonistic function compared with its closest homolog FKBP52 remains enigmatic. Here we review recent structural and biochemical studies of FKBPs as regulators in the Hsp90 machinery. These advances provide important insights into the roles of FKBP51 and FKBP52 in SHR regulation.

Funder

Bundesministerium für Bildung und Forschung

Deutsche Forschungsgemeinschaft

Hessisches Ministerium für Wissenschaft und Kunst

Publisher

Wiley

Subject

Cell Biology,Molecular Biology,Biochemistry

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