Title : A structure-based mutational analysis of cyclophilin 40 identifies key residues in the core tetratricopeptide repeat domain that mediate binding to Hsp90.

Pub. Date : 2002 Oct 25

PMID : 12145316






3 Functional Relationships(s)
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1 Mutational analysis identified five of these residues (Lys-227, Asn-231, Asn-278, Lys-308, and Arg-312) as essential for Hsp90 binding. Lysine Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C
2 Mutational analysis identified five of these residues (Lys-227, Asn-231, Asn-278, Lys-308, and Arg-312) as essential for Hsp90 binding. Lysine Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C
3 The other two residues (Phe-234 and Ser-274) and another three TPR domain residues not definitively associated with the binding groove (Leu-284, Lys-285, and Asp-329) are required for efficient Hsp90 binding. Lysine Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C