4WOH

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

Summary for 4WOH

• Entry DOI: 10.2210/pdb4woh/pdb
• Descriptor: Dual specificity protein phosphatase 22, 4-NITROPHENYL PHOSPHATE, DI(HYDROXYETHYL)ETHER, ... (5 entities in total)
• Functional Keywords: dual specificity phosphatase, jsp-1, pnpp, hydrolase
• Biological source: Homo sapiens (Human)
• Cellular location: Cytoplasm : Q9NRW4
• Total number of polymer chains: 1
• Total formula weight: 18935.28

Authors

Lountos, G.T.,Cherry, S.,Tropea, J.E.,Waugh, D.S. (deposition date: 2014-10-15, release date: 2015-02-18, Last modification date: 2023-09-27)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.34 Å)