Structures of Gα Proteins in Complex with Their Chaperone Reveal Quality Control Mechanisms

Structures of Gα Proteins in Complex with Their Chaperone Reveal Quality Control Mechanisms

Summary: Many chaperones promote nascent polypeptide folding followed by substrate release through ATP-dependent conformational changes. Here we show cryoEM structures of Gα subunit folding intermediates in complex with full-length Ric-8A, a unique chaperone-client system in which substrate release...

Full description

Bibliographic Details
Main Authors: Alpay Burak Seven, Daniel Hilger, Makaía M. Papasergi-Scott, Li Zhang, Qianhui Qu, Brian K. Kobilka, Gregory G. Tall, Georgios Skiniotis
Format: Article
Language:English
Published: Elsevier 2020-03-01
Series:Cell Reports
Online Access:http://www.sciencedirect.com/science/article/pii/S2211124720302606

Internet

http://www.sciencedirect.com/science/article/pii/S2211124720302606

Similar Items