4Y2E

Crystal structure of the catalytic domain of human dual-specificity phosphatase 7 (C232S)

4Y2E の概要

• エントリーDOI: 10.2210/pdb4y2e/pdb
• 分子名称: Dual specificity protein phosphatase 7, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: dual specificity phosphatase, hydrolase
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Cytoplasm: Q16829
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 67424.62

構造登録者

Lountos, G.T.,Austin, B.P.,Tropea, J.E.,Waugh, D.S. (登録日: 2015-02-09, 公開日: 2015-06-03, 最終更新日: 2023-09-27)

主引用文献

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

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: 26057789
DOI: 10.1107/S2053230X1500504X

実験手法

X-RAY DIFFRACTION (1.67 Å)