6D3F

Crystal Structure of the PTP epsilon D2 domain

Summary for 6D3F

• Entry DOI: 10.2210/pdb6d3f/pdb
• Descriptor: Receptor-type tyrosine-protein phosphatase epsilon (2 entities in total)
• Functional Keywords: phosphatase, hydrolase
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 2
• Total formula weight: 64667.56

Authors

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. (deposition date: 2018-04-16, release date: 2018-10-17, Last modification date: 2023-10-04)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.271 Å)