Φορτώνει......
Dimerization and N-terminal domain proximity underlie the function of the molecular chaperone heat shock protein 90
Heat shock protein (hsp)90 functions in a complex chaperoning pathway where its activity is modulated by ATP and by interaction with several co-chaperones. One co-chaperone, p23, binds selectively to the ATP-bound state of hsp90. However, the isolated ATP-binding domain of hsp90 does not bind p23. I...
Αποθηκεύτηκε σε:
| Κύριοι συγγραφείς: | , , , , , , |
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| Μορφή: | Artigo |
| Γλώσσα: | Inglês |
| Έκδοση: |
The National Academy of Sciences
2000
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| Θέματα: | |
| Διαθέσιμο Online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC18797/ https://ncbi.nlm.nih.gov/pubmed/11050175 |
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