RPAP3 provides a flexible scaffold for coupling HSP90 to the human R2TP co-chaperone complex

RPAP3 provides a flexible scaffold for coupling HSP90 to the human R2TP co-chaperone complex

The R2TP/PFDL co-chaperone facilitates assembly of RNA polymerase II and PI3-kinase-like kinases such as mTOR by a so far unknown mechanism. Here authors provide the cryo-EM structure of human R2TP, which shows how RPAP3 serves as a flexible platform to recruit HSP90 to diverse client proteins.

Bibliographic Details
Main Authors: Fabrizio Martino, Mohinder Pal, Hugo Muñoz-Hernández, Carlos F. Rodríguez, Rafael Núñez-Ramírez, David Gil-Carton, Gianluca Degliesposti, J. Mark Skehel, S. Mark Roe, Chrisostomos Prodromou, Laurence H. Pearl, Oscar Llorca
Format: Article
Language:English
Published: Nature Publishing Group 2018-04-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-018-03942-1

Internet

https://doi.org/10.1038/s41467-018-03942-1

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