Structural highlights
Function
[PTN1_HUMAN] Tyrosine-protein phosphatase which acts as a regulator of endoplasmic reticulum unfolded protein response. Mediates dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion.[1] [2]
Publication Abstract from PubMed
The X-ray crystal structure of the complex of protein tyrosine phosphatase 1B with nitrate anion has been determined and modelled quantum-mechanically. Two protomers were present in the structure, one with the mechanistically important WPD loop closed and the other with this loop open. Nitrate was observed bound to each protomer, making close contacts with the S atom of the catalytic cysteine and a tyrosine residue from a crystallographically related protomer.
Nitrate in the active site of protein tyrosine phosphatase 1B is a putative mimetic of the transition state.,Kenny PW, Newman J, Peat TS Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):565-71. doi:, 10.1107/S1399004713031052. Epub 2014 Jan 31. PMID:24531490[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nievergall E, Janes PW, Stegmayer C, Vail ME, Haj FG, Teng SW, Neel BG, Bastiaens PI, Lackmann M. PTP1B regulates Eph receptor function and trafficking. J Cell Biol. 2010 Dec 13;191(6):1189-203. doi: 10.1083/jcb.201005035. Epub 2010, Dec 6. PMID:21135139 doi:10.1083/jcb.201005035
- ↑ Krishnan N, Fu C, Pappin DJ, Tonks NK. H2S-Induced sulfhydration of the phosphatase PTP1B and its role in the endoplasmic reticulum stress response. Sci Signal. 2011 Dec 13;4(203):ra86. doi: 10.1126/scisignal.2002329. PMID:22169477 doi:10.1126/scisignal.2002329
- ↑ Kenny PW, Newman J, Peat TS. Nitrate in the active site of protein tyrosine phosphatase 1B is a putative mimetic of the transition state. Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):565-71. doi:, 10.1107/S1399004713031052. Epub 2014 Jan 31. PMID:24531490 doi:http://dx.doi.org/10.1107/S1399004713031052
