|
|
| Line 3: |
Line 3: |
| | <StructureSection load='4rsu' size='340' side='right'caption='[[4rsu]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='4rsu' size='340' side='right'caption='[[4rsu]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4rsu]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RSU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RSU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4rsu]] is a 12 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=4RSU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RSU FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4j6g|4j6g]], [[4fhq|4fhq]], [[2aw2|2aw2]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TNFSF14, HVEML, LIGHT, UNQ391/PRO726 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), TNFRSF14, HVEA, HVEM, UNQ329/PRO509 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4rsu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rsu OCA], [https://pdbe.org/4rsu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rsu RCSB], [https://www.ebi.ac.uk/pdbsum/4rsu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rsu 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=4rsu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rsu OCA], [https://pdbe.org/4rsu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rsu RCSB], [https://www.ebi.ac.uk/pdbsum/4rsu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rsu ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/TNF14_HUMAN TNF14_HUMAN]] Cytokine that binds to TNFRSF3/LTBR. Binding to the decoy receptor TNFRSF6B modulates its effects. Activates NFKB, stimulates the proliferation of T-cells, and inhibits growth of the adenocarcinoma HT-29. Acts as a receptor for Herpes simplex virus. [[https://www.uniprot.org/uniprot/TNR14_HUMAN TNR14_HUMAN]] Receptor for BTLA. Receptor for TNFSF14/LIGHT and homotrimeric TNFSF1/lymphotoxin-alpha. Involved in lymphocyte activation. Plays an important role in HSV pathogenesis because it enhanced the entry of several wild-type HSV strains of both serotypes into CHO cells, and mediated HSV entry into activated human T-cells.<ref>PMID:8898196</ref>
| + | [https://www.uniprot.org/uniprot/TNF14_HUMAN TNF14_HUMAN] Cytokine that binds to TNFRSF3/LTBR. Binding to the decoy receptor TNFRSF6B modulates its effects. Activates NFKB, stimulates the proliferation of T-cells, and inhibits growth of the adenocarcinoma HT-29. Acts as a receptor for Herpes simplex virus. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 27: |
Line 26: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Almo, S C]] | + | [[Category: Almo SC]] |
| - | [[Category: Bonanno, J B]] | + | [[Category: Bonanno JB]] |
| - | [[Category: Himmel, D]] | + | [[Category: Himmel D]] |
| - | [[Category: IFN, Atoms-to-Animals:.The Immune Function Network]]
| + | [[Category: Liu W]] |
| - | [[Category: Liu, W]] | + | [[Category: Nathenson SG]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Ramagoal UA]] |
| - | [[Category: Nathenson, S G]] | + | |
| - | [[Category: Ramagoal, U A]] | + | |
| - | [[Category: Atoms-to-animals: the immune function network]]
| + | |
| - | [[Category: Cell membrane]]
| + | |
| - | [[Category: Cysteine rich domain]]
| + | |
| - | [[Category: Cytokine]]
| + | |
| - | [[Category: Ifn]]
| + | |
| - | [[Category: Immune system]]
| + | |
| - | [[Category: Immunity]]
| + | |
| - | [[Category: Jelly-roll fold]]
| + | |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: N-glycosylation]]
| + | |
| - | [[Category: Nysgrc]]
| + | |
| - | [[Category: PSI, Protein structure initiative]]
| + | |
| - | [[Category: Psi-biology]]
| + | |
| - | [[Category: Research consortium]]
| + | |
| - | [[Category: Secreted]]
| + | |
| - | [[Category: Secreted protein]]
| + | |
| - | [[Category: Signaling]]
| + | |
| Structural highlights
Function
TNF14_HUMAN Cytokine that binds to TNFRSF3/LTBR. Binding to the decoy receptor TNFRSF6B modulates its effects. Activates NFKB, stimulates the proliferation of T-cells, and inhibits growth of the adenocarcinoma HT-29. Acts as a receptor for Herpes simplex virus.
Publication Abstract from PubMed
HVEM is a TNF (tumor necrosis factor) receptor contributing to a broad range of immune functions involving diverse cell types. It interacts with a TNF ligand, LIGHT, and immunoglobulin (Ig) superfamily members BTLA and CD160. Assessing the functional impact of HVEM binding to specific ligands in different settings has been complicated by the multiple interactions of HVEM and HVEM binding partners. To dissect the molecular basis for multiple functions, we determined crystal structures that reveal the distinct HVEM surfaces that engage LIGHT or BTLA/CD160, including the human HVEM-LIGHT-CD160 ternary complex, with HVEM interacting simultaneously with both binding partners. Based on these structures, we generated mouse HVEM mutants that selectively recognized either the TNF or Ig ligands in vitro. Knockin mice expressing these muteins maintain expression of all the proteins in the HVEM network, yet they demonstrate selective functions for LIGHT in the clearance of bacteria in the intestine and for the Ig ligands in the amelioration of liver inflammation.
HVEM structures and mutants reveal distinct functions of binding to LIGHT and BTLA/CD160.,Liu W, Chou TF, Garrett-Thomson SC, Seo GY, Fedorov E, Ramagopal UA, Bonanno JB, Wang Q, Kim K, Garforth SJ, Kakugawa K, Cheroutre H, Kronenberg M, Almo SC J Exp Med. 2021 Dec 6;218(12). pii: 212735. doi: 10.1084/jem.20211112. Epub 2021 , Oct 28. PMID:34709351[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Liu W, Chou TF, Garrett-Thomson SC, Seo GY, Fedorov E, Ramagopal UA, Bonanno JB, Wang Q, Kim K, Garforth SJ, Kakugawa K, Cheroutre H, Kronenberg M, Almo SC. HVEM structures and mutants reveal distinct functions of binding to LIGHT and BTLA/CD160. J Exp Med. 2021 Dec 6;218(12). pii: 212735. doi: 10.1084/jem.20211112. Epub 2021 , Oct 28. PMID:34709351 doi:http://dx.doi.org/10.1084/jem.20211112
|
