6ntp: Difference between revisions

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'''Unreleased structure'''


The entry 6ntp is ON HOLD  until Paper Publication
==PTP1B Domain of PTP1B-LOV2 Chimera==
 
<StructureSection load='6ntp' size='340' side='right'caption='[[6ntp]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
Authors: Hongdusit, A., Sankaran, B., Zwart, P.H., Fox, J.M.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[6ntp]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NTP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NTP FirstGlance]. <br>
Description: PTPT1B Domain of PTP1B-LOV2 Chimera
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
[[Category: Unreleased Structures]]
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ntp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ntp OCA], [http://pdbe.org/6ntp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ntp RCSB], [http://www.ebi.ac.uk/pdbsum/6ntp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ntp ProSAT]</span></td></tr>
</table>
== Function ==
[[http://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: Large Structures]]
[[Category: Protein-tyrosine-phosphatase]]
[[Category: Fox, J M]]
[[Category: Hongdusit, A]]
[[Category: Sankaran, B]]
[[Category: Sankaran, B]]
[[Category: Fox, J.M]]
[[Category: Zwart, P H]]
[[Category: Zwart, P.H]]
[[Category: Cancer]]
[[Category: Hongdusit, A]]
[[Category: Diabetes]]
[[Category: Hydrolase]]
[[Category: Obesity]]
[[Category: Protein phosphorylation]]
[[Category: Protein tyrosine phosphatase]]
[[Category: Signaling]]

Revision as of 19:11, 22 January 2020

PTP1B Domain of PTP1B-LOV2 ChimeraPTP1B Domain of PTP1B-LOV2 Chimera

Structural highlights

6ntp is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:Protein-tyrosine-phosphatase, with EC number 3.1.3.48
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

6ntp, resolution 1.89Å

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OCA
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