4CSE

PIH N-terminal domain

4CSE の概要

• エントリーDOI: 10.2210/pdb4cse/pdb
• 関連するPDBエントリー: 4CGU 4CGV 4CGW 4CHH 4CKT 4CV4
• 分子名称: PIH1 DOMAIN-CONTAINING PROTEIN 1, TELOMERE LENGTH REGULATION PROTEIN TEL2 HOMOLOG (3 entities in total)
• 機能のキーワード: chaperone, molecular chaperones, multiprotein complexes, phosphorylation
• 由来する生物種: MUS MUSCULUS (HOUSE MOUSE); 詳細
• 細胞内の位置: Cytoplasm (By similarity): Q9DC40
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 32225.79

構造登録者

Morgan, R.M.,Roe, S.M. (登録日: 2014-03-07, 公開日: 2014-05-14, 最終更新日: 2024-10-23)

主引用文献

Pal, M.,Morgan, M.,Phelps, S.E.,Roe, S.M.,Parry-Morris, S.,Downs, J.A.,Polier, S.,Pearl, L.H.,Prodromou, C.
Structural Basis for Phosphorylation-Dependent Recruitment of Tel2 to Hsp90 by Pih1.
Structure, 22:805-, 2014

PubMed Abstract: Client protein recruitment to the Hsp90 system depends on cochaperones that bind the client and Hsp90 simultaneously and facilitate their interaction. Hsp90 involvement in the assembly of snoRNPs, RNA polymerases, PI3-kinase-like kinases, and chromatin remodeling complexes depends on the TTT (Tel2-Tti1-Tti2), and R2TP complexes-consisting of the AAA-ATPases Rvb1 and Rvb2, Tah1 (Spagh/RPAP3 in metazoa), and Pih1 (Pih1D1 in humans)-that together provide the connection to Hsp90. The biochemistry underlying R2TP function is still poorly understood. Pih1 in particular, at the heart of the complex, has not been described at a structural level, nor have the multiple protein-protein interactions it mediates been characterized. Here we present a structural and biochemical analysis of Hsp90-Tah1-Pih1, Hsp90-Spagh, and Pih1D1-Tel2 complexes that reveal a domain in Pih1D1 specific for binding CK2 phosphorylation sites, and together define the structural basis by which the R2TP complex connects the Hsp90 chaperone system to the TTT complex.

PubMed: 24794838
DOI: 10.1016/J.STR.2014.04.001

実験手法

X-RAY DIFFRACTION (3.3 Å)