4en0: Difference between revisions
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==Crystal structure of light== | ==Crystal structure of light== | ||
<StructureSection load='4en0' size='340' side='right' caption='[[4en0]], [[Resolution|resolution]] 2.59Å' scene=''> | <StructureSection load='4en0' size='340' side='right' caption='[[4en0]], [[Resolution|resolution]] 2.59Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HVEML, LIGHT, TNFSF14, UNQ391/PRO726 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HVEML, LIGHT, TNFSF14, UNQ391/PRO726 ([http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4en0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4en0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4en0 RCSB], [http://www.ebi.ac.uk/pdbsum/4en0 PDBsum]</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=4en0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4en0 OCA], [http://pdbe.org/4en0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4en0 RCSB], [http://www.ebi.ac.uk/pdbsum/4en0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4en0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4en0" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Tumor necrosis factor receptor|Tumor necrosis factor receptor]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 11:45, 4 August 2016
Crystal structure of lightCrystal structure of light
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 PubMedLIGHT initiates intracellular signaling via engagement of the two TNF receptors, HVEM and LTbetaR. In humans, LIGHT is neutralized by DcR3, a unique soluble member of the TNFR superfamily, which tightly binds LIGHT and inhibits its interactions with HVEM and LTbetaR. DcR3 also neutralizes two other TNF ligands, FasL and TL1A. Due to its ability to neutralize three distinct different ligands, DcR3 contributes to a wide range of biological and pathological processes, including cancer and autoimmune diseases. However, the mechanisms that support the broad specificity of DcR3 remain to be fully defined. We report the structures of LIGHT and the LIGHT:DcR3 complex, which reveal the structural basis for the DcR3-mediated neutralization of LIGHT and afford insights into DcR3 function and binding promiscuity. Based on these structures, we designed LIGHT mutants with altered affinities for DcR3 and HVEM, which may represent mechanistically informative probe reagents. Mechanistic basis for functional promiscuity in the TNF and TNF receptor superfamilies: structure of the LIGHT:DcR3 assembly.,Liu W, Zhan C, Cheng H, Kumar PR, Bonanno JB, Nathenson SG, Almo SC Structure. 2014 Sep 2;22(9):1252-62. doi: 10.1016/j.str.2014.06.013. Epub 2014, Jul 31. PMID:25087510[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Human
- Almo, S C
- Bonanno, J B
- IFN, Atoms-to-Animals:.The Immune Function Network
- Liu, W
- Structural genomic
- Nathenson, S G
- Patskovsky, Y
- Ramagopal, U A
- Zhan, C
- Atoms-to-animals: the immune function network
- Bind tnf receptor hvem and ltbr
- Cytokine
- Dcr3
- Hvem
- Ifn
- Immunity
- Jelly-roll fold
- Ltbr
- Membrane
- N-glycosylation
- Nysgrc
- Psi-biology
- Secreted protein
- Tnf superfamily