6FDP

NMR structure of the second TPR domain of the human RPAP3 protein in complex with HSP90 peptide DTSRMEEVD

6FDP の概要

• エントリーDOI: 10.2210/pdb6fdp/pdb
• NMR情報: BMRB: 34223
• 分子名称: RNA polymerase II-associated protein 3, Heat shock protein HSP 90-alpha (2 entities in total)
• 機能のキーワード: tpr hsp ruvbl polymerase, chaperone
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 14450.40

構造登録者

Quinternet, M.,Chagot, M.E.,Manival, X. (登録日: 2017-12-26, 公開日: 2018-08-01, 最終更新日: 2024-06-19)

主引用文献

Henri, J.,Chagot, M.E.,Bourguet, M.,Abel, Y.,Terral, G.,Maurizy, C.,Aigueperse, C.,Georgescauld, F.,Vandermoere, F.,Saint-Fort, R.,Behm-Ansmant, I.,Charpentier, B.,Pradet-Balade, B.,Verheggen, C.,Bertrand, E.,Meyer, P.,Cianferani, S.,Manival, X.,Quinternet, M.
Deep Structural Analysis of RPAP3 and PIH1D1, Two Components of the HSP90 Co-chaperone R2TP Complex.
Structure, 26:1196-1209.e8, 2018

PubMed Abstract: RPAP3 and PIH1D1 are part of the HSP90 co-chaperone R2TP complex involved in the assembly process of many molecular machines. In this study, we performed a deep structural investigation of the HSP binding abilities of the two TPR domains of RPAP3. We combined 3D NMR, non-denaturing MS, and ITC techniques with Y2H, IP-LUMIER, FRET, and ATPase activity assays and explain the fundamental role played by the second TPR domain of RPAP3 in the specific recruitment of HSP90. We also established the 3D structure of an RPAP3:PIH1D1 sub-complex demonstrating the need for a 34-residue insertion, specific of RPAP3 isoform 1, for the tight binding of PIH1D1. We also confirm the existence of a complex lacking PIH1D1 in human cells (R2T), which shows differential binding to certain clients. These results highlight similarities and differences between the yeast and human R2TP complexes, and document the diversification of this family of co-chaperone complexes in human.

PubMed: 30033218
DOI: 10.1016/j.str.2018.06.002

実験手法

SOLUTION NMR