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| | <StructureSection load='3se3' size='340' side='right'caption='[[3se3]], [[Resolution|resolution]] 4.00Å' scene=''> | | <StructureSection load='3se3' size='340' side='right'caption='[[3se3]], [[Resolution|resolution]] 4.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3se3]] is a 3 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=3SE3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SE3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3se3]] is a 3 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=3SE3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SE3 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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]] 4.0001Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3s8w|3s8w]], [[3s98|3s98]], [[3s9d|3s9d]], [[3se4|3se4]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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">IFNAR1, IFNAR ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), IFNAR2, IFNABR, IFNARB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3se3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3se3 OCA], [https://pdbe.org/3se3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3se3 RCSB], [https://www.ebi.ac.uk/pdbsum/3se3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3se3 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=3se3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3se3 OCA], [https://pdbe.org/3se3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3se3 RCSB], [https://www.ebi.ac.uk/pdbsum/3se3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3se3 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/INAR1_HUMAN INAR1_HUMAN]] Associates with IFNAR2 to form the type I interferon receptor. Receptor for interferons alpha and beta. Binding to type I IFNs triggers tyrosine phosphorylation of a number of proteins including JAKs, TYK2, STAT proteins and IFNR alpha- and beta-subunits themselves. [[https://www.uniprot.org/uniprot/INAR2_HUMAN INAR2_HUMAN]] Associates with IFNAR1 to form the type I interferon receptor. Receptor for interferons alpha and beta. Involved in IFN-mediated STAT1, STAT2 and STAT3 activation. Isoform 1 and isoform 2 are directly involved in signal transduction due to their association with the TYR kinase, JAK1. Isoform 3 is a potent inhibitor of type I IFN receptor activity.<ref>PMID:8181059</ref> <ref>PMID:7665574</ref> <ref>PMID:7759950</ref> <ref>PMID:11682488</ref> <ref>PMID:12105218</ref>
| + | [https://www.uniprot.org/uniprot/INAR1_HUMAN INAR1_HUMAN] Associates with IFNAR2 to form the type I interferon receptor. Receptor for interferons alpha and beta. Binding to type I IFNs triggers tyrosine phosphorylation of a number of proteins including JAKs, TYK2, STAT proteins and IFNR alpha- and beta-subunits themselves. |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | Type I Interferons (IFNs) are important cytokines for innate immunity against viruses and cancer. Sixteen human type I IFN variants signal through the same cell-surface receptors, IFNAR1 and IFNAR2, yet they can evoke markedly different physiological effects. The crystal structures of two human type I IFN ternary signaling complexes containing IFNalpha2 and IFNomega reveal recognition modes and heterotrimeric architectures that are unique among the cytokine receptor superfamily but conserved between different type I IFNs. Receptor-ligand cross-reactivity is enabled by conserved receptor-ligand "anchor points" interspersed among ligand-specific interactions that "tune" the relative IFN-binding affinities, in an apparent extracellular "ligand proofreading" mechanism that modulates biological activity. Functional differences between IFNs are linked to their respective receptor recognition chemistries, in concert with a ligand-induced conformational change in IFNAR1, that collectively control signal initiation and complex stability, ultimately regulating differential STAT phosphorylation profiles, receptor internalization rates, and downstream gene expression patterns.
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| - | | + | |
| - | Structural linkage between ligand discrimination and receptor activation by type I interferons.,Thomas C, Moraga I, Levin D, Krutzik PO, Podoplelova Y, Trejo A, Lee C, Yarden G, Vleck SE, Glenn JS, Nolan GP, Piehler J, Schreiber G, Garcia KC Cell. 2011 Aug 19;146(4):621-32. PMID:21854986<ref>PMID:21854986</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 3se3" style="background-color:#fffaf0;"></div>
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| | | | |
| | ==See Also== | | ==See Also== |
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| | *[[Interferon receptor 3D structures|Interferon receptor 3D structures]] | | *[[Interferon receptor 3D structures|Interferon receptor 3D structures]] |
| | *[[Multiple sclerosis|Multiple sclerosis]] | | *[[Multiple sclerosis|Multiple sclerosis]] |
| - | == References == | |
| - | <references/> | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Garcia, K C]] | + | [[Category: Garcia KC]] |
| - | [[Category: Thomas, C]] | + | [[Category: Thomas C]] |
| - | [[Category: Extracellular space]]
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| - | [[Category: Immune system receptor]]
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| - | [[Category: Type i interferon signaling complex]]
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