3KD7

Designed TPR module (CTPR390) in complex with its peptide-ligand (Hsp90 peptide)

Summary for 3KD7

• Entry DOI: 10.2210/pdb3kd7/pdb
• Related: 1ELR 1ELW 1NA0 1NA3 2avp 2C2L 3FWV
• Descriptor: CTPR390, Hsp90 MEEVD peptide (3 entities in total)
• Functional Keywords: designed protein, tetratricopeptide repeat (tpr), hsp90 binding, repeat protein, tpr-ligand complex, superhelical structure, de novo protein
• Biological source: UNIDENTIFIED; More
• Total number of polymer chains: 10
• Total formula weight: 75096.93

Authors

Cortajarena, A.L.,Wang, J.,Regan, L. (deposition date: 2009-10-22, release date: 2010-02-02, Last modification date: 2024-11-27)

Primary citation

Cortajarena, A.L.,Wang, J.,Regan, L.
Crystal structure of a designed tetratricopeptide repeat module in complex with its peptide ligand.
Febs J., 277:1058-1066, 2010

PubMed Abstract: Tetratricopeptide repeats (TPRs) are protein domains that mediate key protein-protein interactions in cells. Several TPR domains bind the C-termini of the chaperones heat shock protein (Hsp)90 and/or Hsp70, and exchange of such binding partners is key for the heat shock response. We have previously described the design of a TPR protein that binds tightly and specifically to the C-terminus of Hsp90, and in doing so, is able to inhibit chaperone function in vivo. Here we present the X-ray crystal structure of the designed TPR domain (CTPR390) in complex with its peptide ligand--the C-terminal residues of Hsp90 (peptide MEEVD). This structure reveals two interesting aspects of the TPR modules. First, a new packing arrangement of 3-TPR modules is observed. The TPR units stack against each other in an unusual fashion to form infinite superhelices in the crystal. Second, the structure provides insights into the molecular basis of TPR-ligand recognition.

PubMed: 20089039
DOI: 10.1111/j.1742-4658.2009.07549.x

Experimental method

X-RAY DIFFRACTION (2.85 Å)