6d3f

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Crystal Structure of the PTP epsilon D2 domain

Structural highlights

6d3f is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.271Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PTPRE_HUMAN Isoform 1 plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells. May play a role in osteoclast formation and function (By similarity). Isoform 2 acts as a negative regulator of insulin receptor (IR) signaling in skeletal muscle. Regulates insulin-induced tyrosine phosphorylation of insulin receptor (IR) and insulin receptor substrate 1 (IRS-1), phosphorylation of protein kinase B and glycogen synthase kinase-3 and insulin induced stimulation of glucose uptake (By similarity). Isoform 1 and isoform 2 act as a negative regulator of FceRI-mediated signal transduction leading to cytokine production and degranulation, most likely by acting at the level of SYK to affect downstream events such as phosphorylation of SLP76 and LAT and mobilization of Ca(2+).

Publication Abstract from PubMed

Here, new crystal structures are presented of the isolated membrane-proximal D1 and distal D2 domains of protein tyrosine phosphatase epsilon (PTP), 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 PTP D2 domain (A455N/V457Y/E597D) was also constructed to reconstitute the residues of the PTP 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 PTP D1 domain is also described.

High-resolution crystal structures of the D1 and D2 domains of protein tyrosine phosphatase epsilon for structure-based drug design.,Lountos GT, Raran-Kurussi S, Zhao BM, Dyas BK, Burke TR Jr, Ulrich RG, Waugh DS Acta Crystallogr D Struct Biol. 2018 Oct 1;74(Pt 10):1015-1026. doi:, 10.1107/S2059798318011919. Epub 2018 Oct 2. PMID:30289412[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
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A novel binding pocket in the D2 domain of protein tyrosine phosphatase mu (PTPmu) guides AI screen to identify small molecules that modulate tumour cell adhesion, growth and migration.
Molyneaux et al. (2023)
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See Also

References

  1. ↑ Lountos GT, Raran-Kurussi S, Zhao BM, Dyas BK, Burke TR Jr, Ulrich RG, Waugh DS. 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. 2018 Oct 1;74(Pt 10):1015-1026. doi:, 10.1107/S2059798318011919. Epub 2018 Oct 2. PMID:30289412 doi:http://dx.doi.org/10.1107/S2059798318011919

Contents


PDB ID 6d3f

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