6D4D

Crystal structure of the PTP epsilon D1 domain

6D4D の概要

• エントリーDOI: 10.2210/pdb6d4d/pdb
• 分子名称: Receptor-type tyrosine-protein phosphatase epsilon (2 entities in total)
• 機能のキーワード: phosphatase, hydrolase
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 67831.86

構造登録者

Lountos, G.T.,Raran-Kurussi, S.,Zhao, B.M.,Dyas, B.K.,Austin, B.P.,Burke Jr., T.R.,Ulrich, R.G.,Waugh, D.S. (登録日: 2018-04-18, 公開日: 2018-10-17, 最終更新日: 2024-10-30)

主引用文献

Lountos, G.T.,Raran-Kurussi, S.,Zhao, B.M.,Dyas, B.K.,Burke Jr., T.R.,Ulrich, R.G.,Waugh, D.S.
High-resolution crystal structures of the D1 and D2 domains of protein tyrosine phosphatase epsilon for structure-based drug design.
Acta Crystallogr D Struct Biol, 74:1015-1026, 2018

PubMed Abstract: Here, new crystal structures are presented of the isolated membrane-proximal D1 and distal D2 domains of protein tyrosine phosphatase epsilon (PTPℇ), a protein tyrosine phosphatase that has been shown to play a positive role in the survival of human breast cancer cells. A triple mutant of the PTPℇ D2 domain (A455N/V457Y/E597D) was also constructed to reconstitute the residues of the PTPℇ D1 catalytic domain that are important for phosphatase activity, resulting in only a slight increase in the phosphatase activity compared with the native D2 protein. The structures reported here are of sufficient resolution for structure-based drug design, and a microarray-based assay for high-throughput screening to identify small-molecule inhibitors of the PTPℇ D1 domain is also described.

PubMed: 30289412
DOI: 10.1107/S2059798318011919

実験手法

X-RAY DIFFRACTION (1.765 Å)