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Allostery in the Hsp70 chaperones is transduced by subdomain rotations
Hsp70s are central to protein folding, refolding, and trafficking in organisms ranging from Archae to Homo sapiens, both at normal and at stressed cellular conditions. Hsp70s are comprised of a nucleotide-binding domain (NBD), and a substrate-binding domain (SBD). The nucleotide binding site in the...
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| Hlavní autoři: | , , , , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
2009
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2693909/ https://ncbi.nlm.nih.gov/pubmed/19361428 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.jmb.2009.01.062 |
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