1ELR

Crystal structure of the TPR2A domain of HOP in complex with the HSP90 peptide MEEVD

1ELR の概要

• エントリーDOI: 10.2210/pdb1elr/pdb
• 関連するPDBエントリー: 1ELW
• 分子名称: TPR2A-DOMAIN OF HOP, HSP90-PEPTIDE MEEVD, NICKEL (II) ION, ... (4 entities in total)
• 機能のキーワード: hop, tpr-domain, peptide-complex, helical repeat, hsp90, protein binding, chaperone
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm : P31948
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 16230.96

構造登録者

Scheufler, C.,Brinker, A.,Hartl, F.U.,Moarefi, I. (登録日: 2000-03-14, 公開日: 2000-04-26, 最終更新日: 2024-11-13)

主引用文献

Scheufler, C.,Brinker, A.,Bourenkov, G.,Pegoraro, S.,Moroder, L.,Bartunik, H.,Hartl, F.U.,Moarefi, I.
Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine.
Cell(Cambridge,Mass.), 101:199-210, 2000

PubMed Abstract: The adaptor protein Hop mediates the association of the molecular chaperones Hsp70 and Hsp90. The TPR1 domain of Hop specifically recognizes the C-terminal heptapeptide of Hsp70 while the TPR2A domain binds the C-terminal pentapeptide of Hsp90. Both sequences end with the motif EEVD. The crystal structures of the TPR-peptide complexes show the peptides in an extended conformation, spanning a groove in the TPR domains. Peptide binding is mediated by electrostatic interactions with the EEVD motif, with the C-terminal aspartate acting as a two-carboxylate anchor, and by hydrophobic interactions with residues upstream of EEVD. The hydrophobic contacts with the peptide are critical for specificity. These results explain how TPR domains participate in the ordered assembly of Hsp70-Hsp90 multichaperone complexes.

PubMed: 10786835
DOI: 10.1016/S0092-8674(00)80830-2

実験手法

X-RAY DIFFRACTION (1.9 Å)