2NZ6

Crystal structure of the PTPRJ inactivating mutant C1239S

2NZ6 の概要

• エントリーDOI: 10.2210/pdb2nz6/pdb
• 関連するPDBエントリー: 2CFV
• 分子名称: Receptor-type tyrosine-protein phosphatase eta, NICKEL (II) ION, PHOSPHATE ION, ... (5 entities in total)
• 機能のキーワード: hydrolase receptor type tyrosine phosphatase j, ptprj, glycoprotein, protein phosphatase, structural genomics, structural genomics consortium, sgc, hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cell membrane; Single-pass type I membrane protein: Q12913
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37290.44

構造登録者

Ugochukwu, E.,Barr, A.,Savitsky, P.,Pike, A.C.W.,Bunkoczi, G.,Sundstrom, M.,Weigelt, J.,Arrowsmith, C.H.,Edwards, A.,von Delft, F.,Knapp, S.,Structural Genomics Consortium (SGC) (登録日: 2006-11-22, 公開日: 2006-12-12, 最終更新日: 2023-08-30)

主引用文献

Barr, A.J.,Ugochukwu, E.,Lee, W.H.,King, O.N.,Filippakopoulos, P.,Alfano, I.,Savitsky, P.,Burgess-Brown, N.A.,Muller, S.,Knapp, S.
Large-scale structural analysis of the classical human protein tyrosine phosphatome.
Cell(Cambridge,Mass.), 136:352-363, 2009

PubMed Abstract: Protein tyrosine phosphatases (PTPs) play a critical role in regulating cellular functions by selectively dephosphorylating their substrates. Here we present 22 human PTP crystal structures that, together with prior structural knowledge, enable a comprehensive analysis of the classical PTP family. Despite their largely conserved fold, surface properties of PTPs are strikingly diverse. A potential secondary substrate-binding pocket is frequently found in phosphatases, and this has implications for both substrate recognition and development of selective inhibitors. Structural comparison identified four diverse catalytic loop (WPD) conformations and suggested a mechanism for loop closure. Enzymatic assays revealed vast differences in PTP catalytic activity and identified PTPD1, PTPD2, and HDPTP as catalytically inert protein phosphatases. We propose a "head-to-toe" dimerization model for RPTPgamma/zeta that is distinct from the "inhibitory wedge" model and that provides a molecular basis for inhibitory regulation. This phosphatome resource gives an expanded insight into intrafamily PTP diversity, catalytic activity, substrate recognition, and autoregulatory self-association.

PubMed: 19167335
DOI: 10.1016/j.cell.2008.11.038

実験手法

X-RAY DIFFRACTION (2.3 Å)