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7msj

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Current revision (16:19, 18 October 2023) (edit) (undo)
 
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<StructureSection load='7msj' size='340' side='right'caption='[[7msj]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='7msj' size='340' side='right'caption='[[7msj]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7msj]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7MSJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MSJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7msj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7MSJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MSJ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7msj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7msj OCA], [https://pdbe.org/7msj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7msj RCSB], [https://www.ebi.ac.uk/pdbsum/7msj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7msj ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7msj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7msj OCA], [https://pdbe.org/7msj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7msj RCSB], [https://www.ebi.ac.uk/pdbsum/7msj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7msj ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/TNR14_MOUSE TNR14_MOUSE]] Receptor for four distinct ligands: The TNF superfamily members TNFSF14/LIGHT and homotrimeric LTA/lymphotoxin-alpha and the immunoglobulin superfamily members BTLA and CD160, altogether defining a complex stimulatory and inhibitory signaling network (By similarity). Signals via the TRAF2-TRAF3 E3 ligase pathway to promote immune cell survival and differentiation (PubMed:19915044). Participates in bidirectional cell-cell contact signaling between antigen presenting cells and lymphocytes. In response to ligation of TNFSF14/LIGHT, delivers costimulatory signals to T cells, promoting cell proliferation and effector functions (By similarity). Interacts with CD160 on NK cells, enhancing IFNG production and anti-tumor immune response (PubMed:25711213). In the context of bacterial infection, acts as a signaling receptor on epithelial cells for CD160 from intraepithelial lymphocytes, triggering the production of antimicrobial proteins and proinflammatory cytokines (PubMed:22801499). Upon binding to CD160 on activated CD4+ T cells, downregulates CD28 costimulatory signaling, restricting memory and alloantigen-specific immune response (By similarity). May interact in cis (on the same cell) or in trans (on other cells) with BTLA (PubMed:19915044, PubMed:15568026). In cis interactions, appears to play an immune regulatory role inhibiting in trans interactions in naive T cells to maintain a resting state. In trans interactions, can predominate during adaptive immune response to provide survival signals to effector T cells (PubMed:19915044, PubMed:15568026).[UniProtKB:Q92956]<ref>PMID:15568026</ref> <ref>PMID:19915044</ref> <ref>PMID:22801499</ref> <ref>PMID:25711213</ref>
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[https://www.uniprot.org/uniprot/TNR14_MOUSE TNR14_MOUSE] Receptor for four distinct ligands: The TNF superfamily members TNFSF14/LIGHT and homotrimeric LTA/lymphotoxin-alpha and the immunoglobulin superfamily members BTLA and CD160, altogether defining a complex stimulatory and inhibitory signaling network (By similarity). Signals via the TRAF2-TRAF3 E3 ligase pathway to promote immune cell survival and differentiation (PubMed:19915044). Participates in bidirectional cell-cell contact signaling between antigen presenting cells and lymphocytes. In response to ligation of TNFSF14/LIGHT, delivers costimulatory signals to T cells, promoting cell proliferation and effector functions (By similarity). Interacts with CD160 on NK cells, enhancing IFNG production and anti-tumor immune response (PubMed:25711213). In the context of bacterial infection, acts as a signaling receptor on epithelial cells for CD160 from intraepithelial lymphocytes, triggering the production of antimicrobial proteins and proinflammatory cytokines (PubMed:22801499). Upon binding to CD160 on activated CD4+ T cells, downregulates CD28 costimulatory signaling, restricting memory and alloantigen-specific immune response (By similarity). May interact in cis (on the same cell) or in trans (on other cells) with BTLA (PubMed:19915044, PubMed:15568026). In cis interactions, appears to play an immune regulatory role inhibiting in trans interactions in naive T cells to maintain a resting state. In trans interactions, can predominate during adaptive immune response to provide survival signals to effector T cells (PubMed:19915044, PubMed:15568026).[UniProtKB:Q92956]<ref>PMID:15568026</ref> <ref>PMID:19915044</ref> <ref>PMID:22801499</ref> <ref>PMID:25711213</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 7msj" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 7msj" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Tumor necrosis factor receptor 3D structures|Tumor necrosis factor receptor 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Almo, S C]]
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[[Category: Mus musculus]]
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[[Category: Bonanno, J B]]
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[[Category: Almo SC]]
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[[Category: Fedorov, E]]
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[[Category: Bonanno JB]]
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[[Category: Garrett-Thompson, S C]]
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[[Category: Fedorov E]]
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[[Category: Liu, W]]
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[[Category: Garrett-Thompson SC]]
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[[Category: Ramagopal, U]]
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[[Category: Liu W]]
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[[Category: Cell membrane]]
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[[Category: Ramagopal U]]
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[[Category: Cysteine rich domain]]
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[[Category: Cytokine]]
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[[Category: Immune system]]
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[[Category: Immunity]]
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[[Category: Membrane]]
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[[Category: N-glycosylation]]
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[[Category: Secreted protein]]
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[[Category: Signaling]]
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[[Category: Tnf receptor]]
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Current revision

The crystal structure of mouse HVEM

PDB ID 7msj

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