Escorting Client Proteins to the Hsp90 Molecular Chaperone

Patrik Eickhoff; Alessandro Costa

doi:10.1016/j.str.2017.06.007

Escorting Client Proteins to the Hsp90 Molecular Chaperone

Structure. 2017 Jul 5;25(7):964-965. doi: 10.1016/j.str.2017.06.007.

Authors

Patrik Eickhoff¹, Alessandro Costa²

Affiliations

¹ Macromolecular Machines Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
² Macromolecular Machines Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK. Electronic address: alessandro.costa@crick.ac.uk.

PMID: 28683276
DOI: 10.1016/j.str.2017.06.007

Abstract

The co-chaperone complex R2TP assists Hsp90 in the folding and maturation of client proteins such as phosphatidylinositol-3-kinase-like kinases. In this issue of Structure, Rivera-Calzada, Pal et al. (2017) describe the architecture and catalytic properties of R2TP, providing new insights into the interplay between Hsp90 and its co-chaperones.

Publication types

Comment

MeSH terms

HSP90 Heat-Shock Proteins*
Molecular Chaperones*

Substances

HSP90 Heat-Shock Proteins
Molecular Chaperones

Grants and funding

15852/CRUK_/Cancer Research UK/United Kingdom