7gu5: Difference between revisions

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'''Unreleased structure'''


The entry 7gu5 is ON HOLD
==PanDDA analysis group deposition of ground-state model of PTP1B, using pre-clustering, cluster12==
 
<StructureSection load='7gu5' size='340' side='right'caption='[[7gu5]], [[Resolution|resolution]] 1.52&Aring;' scene=''>
Authors: Mehlman, T., Ginn, H.M., Keedy, D.A.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[7gu5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7GU5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7GU5 FirstGlance]. <br>
Description: PanDDA analysis group deposition of ground-state model of PTP1B, using pre-clustering, cluster12
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.52&#8491;</td></tr>
[[Category: Unreleased Structures]]
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
[[Category: Mehlman, T]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7gu5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7gu5 OCA], [https://pdbe.org/7gu5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7gu5 RCSB], [https://www.ebi.ac.uk/pdbsum/7gu5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7gu5 ProSAT]</span></td></tr>
[[Category: Ginn, H.M]]
</table>
[[Category: Keedy, D.A]]
== Function ==
[https://www.uniprot.org/uniprot/PTN1_HUMAN 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.<ref>PMID:21135139</ref> <ref>PMID:22169477</ref>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Ginn HM]]
[[Category: Keedy DA]]
[[Category: Mehlman T]]

Latest revision as of 14:39, 1 February 2024

PanDDA analysis group deposition of ground-state model of PTP1B, using pre-clustering, cluster12PanDDA analysis group deposition of ground-state model of PTP1B, using pre-clustering, cluster12

Structural highlights

7gu5 is a 1 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 1.52Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

References

  1. ↑ 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
  2. ↑ 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

7gu5, resolution 1.52Å

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OCA
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