3og6: Difference between revisions
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The | ==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=''> | |||
== Structural highlights == | |||
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.097Å</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='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> | |||
== 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. | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:20934432</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3og6" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Interferon 3D structures|Interferon 3D structures]] | |||
*[[Interferon receptor 3D structures|Interferon receptor 3D structures]] | |||
*[[Interleukin 3D structures|Interleukin 3D structures]] | |||
*[[Interleukin receptor 3D structures|Interleukin receptor 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Kotenko SV]] | |||
[[Category: Lei W]] | |||
[[Category: Magracheva E]] | |||
[[Category: Miknis ZJ]] | |||
[[Category: Wlodawer A]] | |||
[[Category: Zdanov A]] | |||
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
FunctionIFNL1_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 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also
References
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