4PSF

PIH1D1 N-terminal domain

4PSF の概要

• エントリーDOI: 10.2210/pdb4psf/pdb
• 関連するPDBエントリー: 4PSI
• 分子名称: PIH1 domain-containing protein 1 (2 entities in total)
• 機能のキーワード: alpha, beta, phospho-binding, tel2, phosphorylation, protein binding
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 30918.95

構造登録者

Smerdon, S.J.,Boulton, S.J.,Stach, L.,Flower, T.G.,Horejsi, Z. (登録日: 2014-03-07, 公開日: 2014-04-23, 最終更新日: 2024-02-28)

主引用文献

Horejsi, Z.,Stach, L.,Flower, T.G.,Joshi, D.,Flynn, H.,Skehel, J.M.,O'Reilly, N.J.,Ogrodowicz, R.W.,Smerdon, S.J.,Boulton, S.J.
Phosphorylation-Dependent PIH1D1 Interactions Define Substrate Specificity of the R2TP Cochaperone Complex.
Cell Rep, 7:19-26, 2014

PubMed Abstract: The R2TP cochaperone complex plays a critical role in the assembly of multisubunit machines, including small nucleolar ribonucleoproteins (snoRNPs), RNA polymerase II, and the mTORC1 and SMG1 kinase complexes, but the molecular basis of substrate recognition remains unclear. Here, we describe a phosphopeptide binding domain (PIH-N) in the PIH1D1 subunit of the R2TP complex that preferentially binds to highly acidic phosphorylated proteins. A cocrystal structure of a PIH-N domain/TEL2 phosphopeptide complex reveals a highly specific phosphopeptide recognition mechanism in which Lys57 and 64 in PIH1D1, along with a conserved DpSDD phosphopeptide motif within TEL2, are essential and sufficient for binding. Proteomic analysis of PIH1D1 interactors identified R2TP complex substrates that are recruited by the PIH-N domain in a sequence-specific and phosphorylation-dependent manner suggestive of a common mechanism of substrate recognition. We propose that protein complexes assembled by the R2TP complex are defined by phosphorylation of a specific motif and recognition by the PIH1D1 subunit.

PubMed: 24656813
DOI: 10.1016/j.celrep.2014.03.013

実験手法

X-RAY DIFFRACTION (1.578 Å)