3KD7

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

3KD7 の概要

• エントリーDOI: 10.2210/pdb3kd7/pdb
• 関連するPDBエントリー: 1ELR 1ELW 1NA0 1NA3 2avp 2C2L 3FWV
• 分子名称: CTPR390, Hsp90 MEEVD peptide (3 entities in total)
• 機能のキーワード: designed protein, tetratricopeptide repeat (tpr), hsp90 binding, repeat protein, tpr-ligand complex, superhelical structure, de novo protein
• 由来する生物種: UNIDENTIFIED; 詳細
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 75096.93

構造登録者

Cortajarena, A.L.,Wang, J.,Regan, L. (登録日: 2009-10-22, 公開日: 2010-02-02, 最終更新日: 2024-11-27)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.85 Å)