4WOH

Structure of of human dual-specificity phosphatase 22 (E24A/K28A/K30A/C88S) complexed with 4-nitrophenolphosphate

4WOH の概要

• エントリーDOI: 10.2210/pdb4woh/pdb
• 分子名称: Dual specificity protein phosphatase 22, 4-NITROPHENYL PHOSPHATE, DI(HYDROXYETHYL)ETHER, ... (5 entities in total)
• 機能のキーワード: dual specificity phosphatase, jsp-1, pnpp, hydrolase
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Cytoplasm : Q9NRW4
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18935.28

構造登録者

Lountos, G.T.,Cherry, S.,Tropea, J.E.,Waugh, D.S. (登録日: 2014-10-15, 公開日: 2015-02-18, 最終更新日: 2023-09-27)

主引用文献

Lountos, G.T.,Cherry, S.,Tropea, J.E.,Waugh, D.S.
Structural analysis of human dual-specificity phosphatase 22 complexed with a phosphotyrosine-like substrate.
Acta Crystallogr.,Sect.F, 71:199-205, 2015

PubMed Abstract: 4-Nitrophenyl phosphate (p-nitrophenyl phosphate, pNPP) is widely used as a small molecule phosphotyrosine-like substrate in activity assays for protein tyrosine phosphatases. It is a colorless substrate that upon hydrolysis is converted to a yellow 4-nitrophenolate ion that can be monitored by absorbance at 405 nm. Therefore, the pNPP assay has been widely adopted as a quick and simple method to assess phosphatase activity and is also commonly used in assays to screen for inhibitors. Here, the first crystal structure is presented of a dual-specificity phosphatase, human dual-specificity phosphatase 22 (DUSP22), in complex with pNPP. The structure illuminates the molecular basis for substrate binding and may also facilitate the structure-assisted development of DUSP22 inhibitors.

PubMed: 25664796
DOI: 10.1107/S2053230X15000217

実験手法

X-RAY DIFFRACTION (1.34 Å)