Chargement en cours...
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...
Enregistré dans:
| Auteurs principaux: | , , , , |
|---|---|
| Format: | Artigo |
| Langue: | Inglês |
| Publié: |
Cold Spring Harbor Laboratory Press
2006
|
| Sujets: | |
| Accès en ligne: | 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 |
| Tags: |
Ajouter un tag
Pas de tags, Soyez le premier à ajouter un tag!
|