Ontology highlight
ABSTRACT:
SUBMITTER: Lee JH
PROVIDER: S-EPMC4534244 | biostudies-literature | 2015 Aug
REPOSITORIES: biostudies-literature
Lee Jung Ho JH Zhang Dongyu D Hughes Christopher C Okuno Yusuke Y Sekhar Ashok A Cavagnero Silvia S
Proceedings of the National Academy of Sciences of the United States of America 20150720 31
The molecular chaperone heat shock protein 70 (Hsp70) plays a vital role in cellular processes, including protein folding and assembly, and helps prevent aggregation under physiological and stress-related conditions. Although the structural changes undergone by full-length client proteins upon interaction with DnaK (i.e., Escherichia coli Hsp70) are fundamental to understand chaperone-mediated protein folding, these changes are still largely unexplored. Here, we show that multiple conformations ...[more]