In vitro evidence that hsp90 contains two independent chaperone sites

摘要: Hsp90 is an abundant and constitutively expressed stress protein molecular chaperone. Here we dissected human hsp90 into three major domains to identify the putative chaperone site at which binds unfolded polypeptide. Surprisingly, both N-terminal C-terminal domain of prevent aggregation denatured polypeptides. The activity N-domain inhibited by geldanamycin, a specific inhibitor hsp90-mediated refolding. While suppress aggregation, only C-domain antigenic peptide derived from VSV G. Based on these results, may be first contain two independent sites with differential specificity.