Fig. 1. Schematic and linear representation of the domain structure and co-chaperone-binding sites of Hsp70 and Hsp90. The amino-acid residue numbers, domains and co-chaperone-binding sites are indicated. (A) Domain structure of human Hsp70. The C-terminal EEVD motif is characteristic for cytosolic Hsp70s and is involved in binding of TPR-domain-containing proteins. (B) Domain structure of human Hsp90. The C-terminal MEEVD motif is involved in binding of TPR-domain-containing proteins. Binding sites of co-chaperones on Hsp90 are a composite of sites of interaction for mammalian and yeast Hsp90 [adapted from previous reports (Chen and Smith, 1998; Grammatikakis et al., 1999; Young et al., 2001)].

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