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![[Figure 1]](dw5132fig1mag.jpg)
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Figure 1
Structures of Tah1 and AIP. (a) Secondary-structure cartoon of the Tah1 TPR-domain dimer (cyan and green). The fifth helix of one TPR domain intercalates between the fourth and fifth helices of the other, generating an effective six-helix two-TPR-domain structure. The bound Hsp90 C-terminal peptides are shown as magenta sticks. Helices are numbered 1–5 and M represents the conserved methionine residue of the EDASRMEEVD peptide (only SRMEEVD was visible), now bound in a hydrophobic pocket formed by amino-acid residues Val74, Ser78, Lys79, Gln81, Tyr82 and Arg83 of Tah1. (b) Secondary-structure cartoon of the monomeric TPR domain of Tah1 (yellow) with bound SRMEEVD peptide derived from the C-terminus of Hsp90 (green sticks). Helices are numbered 1–5 and M represents the conserved methionine residue of the EDASRMEEVD peptide (only SRMEEVD was visible). (c) Secondary-structure cartoon of the TPR domain of AIP (yellow) bound to the SRMEEVD peptide derived from the C-terminus of Hsp90 (green sticks). Helices are numbered 1–5 and M represents the conserved methionine residue of the EDASRMEEVD peptide (only SRMEEVD was visible). |
![[Figure 1]](dw5132fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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