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| | ==human IFNAR1== | | ==human IFNAR1== |
| - | <StructureSection load='3s98' size='340' side='right' caption='[[3s98]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='3s98' size='340' side='right'caption='[[3s98]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3s98]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S98 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3S98 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3s98]] is a 1 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=3S98 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S98 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 1.9Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3s8w|3s8w]], [[3s9d|3s9d]]</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=3s98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s98 OCA], [https://pdbe.org/3s98 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s98 RCSB], [https://www.ebi.ac.uk/pdbsum/3s98 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s98 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IFNAR1, IFNAR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
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| - | <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=3s98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s98 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3s98 RCSB], [http://www.ebi.ac.uk/pdbsum/3s98 PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == 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. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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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 3s98" style="background-color:#fffaf0;"></div> |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[IFNAR1 Nana|IFNAR1 Nana]]
| + | *[[Interferon receptor 3D structures|Interferon receptor 3D structures]] |
| - | *[[Interactive 3D Complements in Proteopedia|Interactive 3D Complements in Proteopedia]]
| + | |
| - | *[[Interferon receptor|Interferon receptor]] | + | |
| | *[[Multiple sclerosis|Multiple sclerosis]] | | *[[Multiple sclerosis|Multiple sclerosis]] |
| | == References == | | == References == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| - | [[Category: Garcia, K C]] | + | [[Category: Large Structures]] |
| - | [[Category: Thomas, C]] | + | [[Category: Garcia KC]] |
| - | [[Category: Extracellular space]] | + | [[Category: Thomas C]] |
| - | [[Category: Fibronectin type iii]]
| + | |
| - | [[Category: Human]]
| + | |
| - | [[Category: Ifnar1]]
| + | |
| - | [[Category: Receptor chain]]
| + | |
| - | [[Category: Signaling protein receptor]]
| + | |
| - | [[Category: Type i interferon receptor chain]]
| + | |
| - | [[Category: Type i interferon]]
| + | |
| Structural highlights
Function
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.
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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. Structural Linkage between Ligand Discrimination and Receptor Activation by Type I Interferons. Cell. 2011 Aug 19;146(4):621-32. PMID:21854986 doi:10.1016/j.cell.2011.06.048
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