Figure 1From: The stress responsive and morphologically regulated hsp90 gene from Paracoccidioides brasiliensis is essential to cell viabilityClustalW alignment of PbHSP90 and other HSP90 family proteins. The Pbhsp90 ORF was translated and aligned with Saccharomyces cerevisiae (Hsp82p, accession number [GenBank: NP_015084.1]) and Homo sapiens (HSP90β, accession number [GenBank: AAQ63401.1]) homologues using ClustalW. Shaded amino acid residues are involved in the binding of either ATP/ADP or geldanamycin in S. cerevisiae [27]. The N-terminal MEEVD motif (bold) is the binding site for the TPR domain of co-chaperones. A total of 400 out of the 706 amino acid residues are conserved across the three species.Back to article page