NDLI: Structural analysis of human dual-specificity phosphatase 22 complexed with a phosphotyrosine-like substrate.

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Year: 2015 Volume: 71 Issue: Part 1

Year: 2014 Volume: 70

Structural analysis of human dual-specificity phosphatase 22 complexed with a phosphotyrosine-like substrate.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Lountos, George T. Cherry, Scott Tropea, Joseph E. Waugh, David S.
Description	Country affiliation: United States Author Affiliation: Lountos GT ( Basic Science Program, Leidos Biomedical Research Inc., Frederick National Laboratory for Cancer Research, Frederick, MD 21702, USA.); Cherry S ( Macromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute, Frederick, MD 21702, USA.); Tropea JE ( Macromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute, Frederick, MD 21702, USA.); Waugh DS ( Macromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute, Frederick, MD 21702, USA.)
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.
File Format	HTM / HTML
ISSN	2053230X
DOI	10.1107/S2053230X15000217
Journal	Acta Crystallographica Section F Structural Biology Communications
Issue Number	Pt 2
Volume Number	71
Language	English
Publisher	IUCr
Publisher Date	2015-02-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Analytical Chemistry Dual-specificity Phosphatases Chemistry Mitogen-activated Protein Kinase Phosphatases Phosphotyrosine Catalytic Domain Crystallography, X-ray Models, Molecular Nitrophenols Organophosphorus Compounds Protein Structure, Secondary Substrate Specificity Research Support, N.i.h., Extramural Research Support, N.i.h., Intramural Research Support, U.s. Gov't, Non-p.h.s.
Content Type	Text
Resource Type	Article
Subject	Genetics Structural Biology Medicine Biochemistry Biophysics Condensed Matter Physics

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