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An unexpected second binding site for polypeptide substrates is essential for Hsp70 chaperone activity
Heat shock proteins of 70 kDa (Hsp70s) are ubiquitous and highly conserved molecular chaperones. They play multiple essential roles in assisting with protein folding and maintaining protein homeostasis. Their chaperone activity has been proposed to require several rounds of binding to and release of...
Uloženo v:
| Vydáno v: | J Biol Chem |
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| Hlavní autoři: | , , , , , , , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
American Society for Biochemistry and Molecular Biology
2020
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6956537/ https://ncbi.nlm.nih.gov/pubmed/31806707 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.RA119.009686 |
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