| Literature DB >> 26057789 |
George T Lountos1, Brian P Austin2, Joseph E Tropea2, David S Waugh2.
Abstract
Human 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 Å 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.Entities:
Keywords: DUSP; DUSP7; MAP kinase phosphatase; PTP; dual-specificity phosphatase
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Year: 2015 PMID: 26057789 PMCID: PMC4461324 DOI: 10.1107/S2053230X1500504X
Source DB: PubMed Journal: Acta Crystallogr F Struct Biol Commun ISSN: 2053-230X Impact factor: 1.056