3og6: Difference between revisions

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<StructureSection load='3og6' size='340' side='right'caption='[[3og6]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='3og6' size='340' side='right'caption='[[3og6]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3og6]] is a 2 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=3OG6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OG6 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3og6]] is a 2 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=3OG6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OG6 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.097&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3hhc|3hhc]], [[3g9v|3g9v]], [[3og4|3og4]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IFNL1, IL29, ZCYTO21 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), hCG_1982865, IL28RA, RP11-10N16.1-001 ([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'>[https://proteopedia.org/fgij/fg.htm?mol=3og6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3og6 OCA], [https://pdbe.org/3og6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3og6 RCSB], [https://www.ebi.ac.uk/pdbsum/3og6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3og6 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=3og6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3og6 OCA], [https://pdbe.org/3og6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3og6 RCSB], [https://www.ebi.ac.uk/pdbsum/3og6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3og6 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/IFNL1_HUMAN 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. [[https://www.uniprot.org/uniprot/INLR1_HUMAN 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.<ref>PMID:12521379</ref> <ref>PMID:12469119</ref> <ref>PMID:12483210</ref> 
[https://www.uniprot.org/uniprot/IFNL1_HUMAN 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.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Kotenko, S V]]
[[Category: Kotenko SV]]
[[Category: Lei, W]]
[[Category: Lei W]]
[[Category: Magracheva, E]]
[[Category: Magracheva E]]
[[Category: Miknis, Z J]]
[[Category: Miknis ZJ]]
[[Category: Wlodawer, A]]
[[Category: Wlodawer A]]
[[Category: Zdanov, A]]
[[Category: Zdanov A]]
[[Category: Beta-sandwich]]
[[Category: Cytokine signaling]]
[[Category: Cytokine-cytokine receptor complex]]
[[Category: Fibronectin type iii domain]]
[[Category: Helical bundle]]
[[Category: Membrane]]

Latest revision as of 12:38, 6 September 2023

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

3og6 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.097Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

Publication Abstract from PubMed

Interferon (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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Miknis Z, Magracheva E, Li W, Zdanov A, Kotenko SV, Wlodawer A. Crystal Structure of Human Interferon-lambda1 in Complex with Its High-Affinity Receptor Interferon-lambdaR1. J Mol Biol. 2010 Oct 8. PMID:20934432 doi:10.1016/j.jmb.2010.09.068

3og6, resolution 2.10Å

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