4Y2E
Crystal structure of the catalytic domain of human dual-specificity phosphatase 7 (C232S)
Summary for 4Y2E
| Entry DOI | 10.2210/pdb4y2e/pdb |
| Descriptor | Dual specificity protein phosphatase 7, PHOSPHATE ION (3 entities in total) |
| Functional Keywords | dual specificity phosphatase, hydrolase |
| Biological source | Homo sapiens (Human) |
| Cellular location | Cytoplasm: Q16829 |
| Total number of polymer chains | 4 |
| Total formula weight | 67424.62 |
| Authors | Lountos, G.T.,Austin, B.P.,Tropea, J.E.,Waugh, D.S. (deposition date: 2015-02-09, release date: 2015-06-03, Last modification date: 2023-09-27) |
| Primary citation | Lountos, G.T.,Austin, B.P.,Tropea, J.E.,Waugh, D.S. Structure of human dual-specificity phosphatase 7, a potential cancer drug target. Acta Crystallogr.,Sect.F, 71:650-656, 2015 Cited by PubMed 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. PubMed: 26057789DOI: 10.1107/S2053230X1500504X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.67 Å) |
Structure validation
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