1n6v
From Proteopedia
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==Average structure of the interferon-binding ectodomain of the human type I interferon receptor== | ==Average structure of the interferon-binding ectodomain of the human type I interferon receptor== | ||
| - | <StructureSection load='1n6v' size='340' side='right'caption='[[1n6v | + | <StructureSection load='1n6v' size='340' side='right'caption='[[1n6v]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1n6v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1n6v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N6V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N6V FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1n6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n6v OCA], [https://pdbe.org/1n6v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n6v RCSB], [https://www.ebi.ac.uk/pdbsum/1n6v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n6v 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=1n6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n6v OCA], [https://pdbe.org/1n6v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n6v RCSB], [https://www.ebi.ac.uk/pdbsum/1n6v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n6v ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [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> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1n6v ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1n6v ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The potent antiviral and antiproliferative activities of human type I interferons (IFNs) are mediated by a single receptor comprising two subunits, IFNAR1 and IFNAR2. The structure of the IFNAR2 IFN binding ectodomain (IFNAR2-EC), the first helical cytokine receptor structure determined in solution, reveals the molecular basis for IFN binding. The atypical perpendicular orientation of its two fibronectin domains explains the lack of C domain involvement in ligand binding. A model of the IFNAR2-EC/IFNalpha2 complex based on double mutant cycle-derived constraints uncovers an extensive and predominantly aliphatic hydrophobic patch on the receptor that interacts with a matching hydrophobic surface of IFNalpha2. An adjacent motif of alternating charged side chains guides the two proteins into a tight complex. The binding interface may account for crossreactivity and ligand specificity of the receptor. This molecular description of IFN binding should be invaluable for study and design of IFN-based biomedical agents. | ||
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| - | The human type I interferon receptor: NMR structure reveals the molecular basis of ligand binding.,Chill JH, Quadt SR, Levy R, Schreiber G, Anglister J Structure. 2003 Jul;11(7):791-802. PMID:12842042<ref>PMID:12842042</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1n6v" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Anglister | + | [[Category: Anglister J]] |
| - | [[Category: Chill | + | [[Category: Chill JH]] |
| - | [[Category: Levy | + | [[Category: Levy R]] |
| - | [[Category: Quadt | + | [[Category: Quadt SR]] |
| - | [[Category: Schreiber | + | [[Category: Schreiber G]] |
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Revision as of 08:46, 10 April 2024
Average structure of the interferon-binding ectodomain of the human type I interferon receptor
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