Structural analysis of human dual-specificity phosphatase 22 complexed with a phosphotyrosine-like substrate.
Acta Crystallogr F Struct Biol Commun
; 71(Pt 2): 199-205, 2015 Feb.
Article
em En
| MEDLINE
| ID: mdl-25664796
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.
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Base de dados:
MEDLINE
Assunto principal:
Fosfotirosina
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Fosfatases da Proteína Quinase Ativada por Mitógeno
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Fosfatases de Especificidade Dupla
Idioma:
En
Ano de publicação:
2015
Tipo de documento:
Article