Hsp70 Forms Antiparallel Dimers Stabilized by Post-translational Modifications to Position Clients for Transfer to Hsp90
Protein folding in cells is regulated by networks of chaperones, including the heat shock protein 70 (Hsp70) system, which consists of the Hsp40 cochaperone and a nucleotide exchange factor. Hsp40 mediates complex formation between Hsp70 and client proteins prior to interaction with Hsp90. We used m...
| Main Authors: | , , , , , , , , , , |
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| Format: | Online |
| Language: | English |
| Published: |
Cell Press
2015
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| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4431665/ |