Structural highlights
Function
DUS22_HUMAN Activates the Jnk signaling pathway. Dephosphorylates and deactivates p38 and stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) (By similarity).[1]
Publication Abstract from PubMed
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.
Structural analysis of human dual-specificity phosphatase 22 complexed with a phosphotyrosine-like substrate.,Lountos GT, Cherry S, Tropea JE, Waugh DS Acta Crystallogr F Struct Biol Commun. 2015 Feb;71(Pt 2):199-205. doi:, 10.1107/S2053230X15000217. Epub 2015 Jan 28. PMID:25664796[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Shen Y, Luche R, Wei B, Gordon ML, Diltz CD, Tonks NK. Activation of the Jnk signaling pathway by a dual-specificity phosphatase, JSP-1. Proc Natl Acad Sci U S A. 2001 Nov 20;98(24):13613-8. PMID:11717427 doi:http://dx.doi.org/10.1073/pnas.231499098
- ↑ Lountos GT, Cherry S, Tropea JE, Waugh DS. Structural analysis of human dual-specificity phosphatase 22 complexed with a phosphotyrosine-like substrate. Acta Crystallogr F Struct Biol Commun. 2015 Feb;71(Pt 2):199-205. doi:, 10.1107/S2053230X15000217. Epub 2015 Jan 28. PMID:25664796 doi:http://dx.doi.org/10.1107/S2053230X15000217
