3og6: Difference between revisions
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==The crystal structure of human interferon lambda 1 complexed with its high affinity receptor in space group P212121== | ==The crystal structure of human interferon lambda 1 complexed with its high affinity receptor in space group P212121== | ||
<StructureSection load='3og6' size='340' side='right' caption='[[3og6]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='3og6' size='340' side='right' caption='[[3og6]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3og6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3og6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OG6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OG6 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <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"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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">[[3hhc|3hhc]], [[3g9v|3g9v]], [[3og4|3og4]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3hhc|3hhc]], [[3g9v|3g9v]], [[3og4|3og4]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IFNL1, IL29, ZCYTO21 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IFNL1, IL29, ZCYTO21 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), hCG_1982865, IL28RA, RP11-10N16.1-001 ([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=3og6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3og6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3og6 RCSB], [http://www.ebi.ac.uk/pdbsum/3og6 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=3og6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3og6 OCA], [http://pdbe.org/3og6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3og6 RCSB], [http://www.ebi.ac.uk/pdbsum/3og6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3og6 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 3og6" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Human]] | ||
[[Category: Kotenko, S V]] | [[Category: Kotenko, S V]] | ||
[[Category: Lei, W]] | [[Category: Lei, W]] | ||
Revision as of 23:15, 4 August 2016
The crystal structure of human interferon lambda 1 complexed with its high affinity receptor in space group P212121The crystal structure of human interferon lambda 1 complexed with its high affinity receptor in space group P212121
Structural highlights
Function[IFNL1_HUMAN] Cytokine with immunomodulatory activity. May play a role in antiviral immunity. Up-regulates MHC class I antigen expression. Ligand for the heterodimeric class II cytokine receptor composed of IL10RB and IFNLR1. The ligand/receptor complex seems to signal through the Jak-STAT pathway. [INLR1_HUMAN] The IFNLR1/IL10RB dimer is a receptor for IFNL1, IFNL2 and IFNL3. The ligand/receptor complex seems to signal through the Jak-STAT pathway. Seems not to be essential for early virus-activated host defense in vaginal infection, but plays an important role in Toll-like receptor (TLR)-induced antiviral defense. Plays a significant role in the antiviral immune defense in the intestinal epithelium.[1] [2] [3] Publication Abstract from PubMedInterferon (IFN)-lambda1 [also known as interleukin (IL)-29] belongs to the recently discovered group of type III IFNs. All type III IFNs initiate signaling processes through formation of specific heterodimeric receptor complexes consisting of IFN-lambdaR1 and IL-10R2. We have determined the structure of human IFN-lambda1 complexed with human IFN-lambdaR1, a receptor unique to type III IFNs. The overall structure of IFN-lambda1 is topologically similar to the structure of IL-10 and other members of the IL-10 family of cytokines. IFN-lambdaR1 consists of two distinct domains having fibronectin type III topology. The ligand-receptor interface includes helix A, loop AB, and helix F on the IFN site, as well as loops primarily from the N-terminal domain and inter-domain hinge region of IFN-lambdaR1. Composition and architecture of the interface that includes only a few direct hydrogen bonds support an idea that long-range ionic interactions between ligand and receptor govern the process of initial recognition of the molecules while hydrophobic interactions finalize it. Crystal Structure of Human Interferon-lambda1 in Complex with Its High-Affinity Receptor Interferon-lambdaR1.,Miknis Z, Magracheva E, Li W, Zdanov A, Kotenko SV, Wlodawer A J Mol Biol. 2010 Oct 8. PMID:20934432[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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