3s98: Difference between revisions
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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 [ | <table><tr><td colspan='2'>[[3s98]] is a 1 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=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='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='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='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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3s8w|3s8w]], [[3s9d|3s9d]]</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]], [[3s9d|3s9d]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IFNAR1, IFNAR ([ | <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])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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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== | ||
*[[Interferon receptor 3D structures|Interferon receptor 3D structures]] | |||
*[[Interferon receptor|Interferon receptor]] | |||
*[[Multiple sclerosis|Multiple sclerosis]] | *[[Multiple sclerosis|Multiple sclerosis]] | ||
== References == | == References == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Garcia, K C]] | [[Category: Garcia, K C]] | ||
[[Category: Thomas, C]] | [[Category: Thomas, C]] | ||
[[Category: Extracellular space]] | [[Category: Extracellular space]] | ||
[[Category: Fibronectin type iii]] | [[Category: Fibronectin type iii]] | ||
[[Category: Ifnar1]] | [[Category: Ifnar1]] | ||
[[Category: Receptor chain]] | [[Category: Receptor chain]] |
Revision as of 10:47, 29 June 2022
human IFNAR1human IFNAR1
Structural highlights
Publication Abstract from PubMedType 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 AlsoReferences
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