4woh: Difference between revisions

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== Function ==

[[http://www.uniprot.org/uniprot/DUS22_HUMAN 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).<ref>PMID:11717427</ref>

== 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<ref>PMID:25664796</ref>

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

== References ==

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 == Function ==
 [[http://www.uniprot.org/uniprot/DUS22_HUMAN 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).<ref>PMID:11717427</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+-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<ref>PMID:25664796</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
 == References ==
 <references/>