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Identification of novel quaternary domain interactions in the Hsp90 chaperone, GRP94
The structural basis for the coupling of ATP binding and hydrolysis to chaperone activity remains a central question in Hsp90 biology. By analogy to MutL, ATP binding to Hsp90 is thought to promote intramolecular N-terminal dimerization, yielding a molecular clamp functioning in substrate protein ac...
Tallennettuna:
| Päätekijät: | , , , , |
|---|---|
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
Cold Spring Harbor Laboratory Press
2006
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2242539/ https://ncbi.nlm.nih.gov/pubmed/16731965 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1110/ps.052065106 |
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