4y2e
Crystal structure of the catalytic domain of human dual-specificity phosphatase 7 (C232S)Crystal structure of the catalytic domain of human dual-specificity phosphatase 7 (C232S)
Structural highlights
FunctionDUS7_HUMAN Regulates the activity of the MAP kinase family in response to changes in the cellular environment. PYST2-S may act as a negative regulator of PYST2-L although it is unclear whether this is by competing for transcription, translation or activation factors.[1] Publication Abstract from PubMedHuman dual-specificity phosphatase 7 (DUSP7/Pyst2) is a 320-residue protein that belongs to the mitogen-activated protein kinase phosphatase (MKP) subfamily of dual-specificity phosphatases. Although its precise biological function is still not fully understood, previous reports have demonstrated that DUSP7 is overexpressed in myeloid leukemia and other malignancies. Therefore, there is interest in developing DUSP7 inhibitors as potential therapeutic agents, especially for cancer. Here, the purification, crystallization and structure determination of the catalytic domain of DUSP7 (Ser141-Ser289/C232S) at 1.67 A resolution are reported. The structure described here provides a starting point for structure-assisted inhibitor-design efforts and adds to the growing knowledge base of three-dimensional structures of the dual-specificity phosphatase family. Structure of human dual-specificity phosphatase 7, a potential cancer drug target.,Lountos GT, Austin BP, Tropea JE, Waugh DS Acta Crystallogr F Struct Biol Commun. 2015 Jun 1;71(Pt 6):650-6. doi:, 10.1107/S2053230X1500504X. Epub 2015 May 20. PMID:26057789[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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