Ontology highlight
ABSTRACT:
SUBMITTER: Morgan RM
PROVIDER: S-EPMC4427203 | biostudies-literature | 2015 May
REPOSITORIES: biostudies-literature
Morgan Rhodri M L RM Pal Mohinder M Roe S Mark SM Pearl Laurence H LH Prodromou Chrisostomos C
Acta crystallographica. Section D, Biological crystallography 20150425 Pt 5
Specific co-chaperone adaptors facilitate the recruitment of client proteins to the Hsp90 system. Tah1 binds the C-terminal conserved MEEVD motif of Hsp90, thus linking an eclectic set of client proteins to the R2TP complex for their assembly and regulation by Hsp90. Rather than the normal complement of seven α-helices seen in other tetratricopeptide repeat (TPR) domains, Tah1 unusually consists of the first five only. Consequently, the methionine of the MEEVD peptide remains exposed to solvent ...[more]