Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2016 Sep 30;3:63. doi: 10.3389/fmolb.2016.00063

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

Copyright © 2016 Ruggieri, Saredi, Zanotti, Pasanisi, Maggi and Mora.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

PMC Copyright notice

The Hsp40-Hsp70 cycle. Hsp40 co-chaperone forms complexes with unfolded or non- native proteins delivering them to Hsp70. The interaction between Hsp40 and the ATP-bound Hsp70 takes place through the J-domain. The client protein transiently interacts with the Hsp70 and the interaction is stabilized by a conformational change in Hsp70 caused by the hydrolysis of ATP which, in turn, is stimulated by both Hsp40 and client protein. Hsp40 is then released. A nucleotide exchange factor (NEF) then binds Hsp70 (having more affinity for the ADP-bound form compared to the ATP form), stimulating the dissociation of ADP through a conformational change in Hsp70. An ATP molecule is bound again to Hsp70 because of its higher cellular concentration, causing the release of the client protein. The system is then ready for a new cycle (Kampinga and Craig, 2010).