3un9: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3un9]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UN9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UN9 FirstGlance]. <br> | <table><tr><td colspan='2'>[[3un9]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UN9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UN9 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PT:PLATINUM+(II)+ION'>PT</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PT:PLATINUM+(II)+ION'>PT</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NLRX1, NOD26, NOD5, NOD9 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NLRX1, NOD26, NOD5, NOD9 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3un9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3un9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3un9 RCSB], [http://www.ebi.ac.uk/pdbsum/3un9 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=3un9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3un9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3un9 RCSB], [http://www.ebi.ac.uk/pdbsum/3un9 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/NLRX1_HUMAN NLRX1_HUMAN]] Participates in antiviral signaling. Acts as a negative regulator of MAVS-mediated antiviral responses, through the inhibition of the virus-induced RLH (RIG-like helicase)-MAVS interaction (PubMed:18200010). Has no inhibitory function on NF-Kappa-B and type 1 interferon signaling pathways, but enhances NF-Kappa-B and JUN N-terminal kinase dependent signaling through the production of reactive oxygen species (PubMed:18219313).<ref>PMID:18219313</ref> <ref>PMID:18200010</ref> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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Structure and Functional Characterization of the RNA-Binding Element of the NLRX1 Innate Immune Modulator.,Hong M, Yoon SI, Wilson IA Immunity. 2012 Mar 23;36(3):337-47. Epub 2012 Mar 1. PMID:22386589<ref>PMID:22386589</ref> | Structure and Functional Characterization of the RNA-Binding Element of the NLRX1 Innate Immune Modulator.,Hong M, Yoon SI, Wilson IA Immunity. 2012 Mar 23;36(3):337-47. Epub 2012 Mar 1. PMID:22386589<ref>PMID:22386589</ref> | ||
From | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
== References == | == References == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Hong, M | [[Category: Hong, M]] | ||
[[Category: Wilson, I A | [[Category: Wilson, I A]] | ||
[[Category: Yoon, S I | [[Category: Yoon, S I]] | ||
[[Category: Antiviral signaling]] | [[Category: Antiviral signaling]] | ||
[[Category: Ikk]] | [[Category: Ikk]] | ||
Revision as of 18:51, 24 December 2014
Crystal structure of an immune receptorCrystal structure of an immune receptor
Structural highlights
Function[NLRX1_HUMAN] Participates in antiviral signaling. Acts as a negative regulator of MAVS-mediated antiviral responses, through the inhibition of the virus-induced RLH (RIG-like helicase)-MAVS interaction (PubMed:18200010). Has no inhibitory function on NF-Kappa-B and type 1 interferon signaling pathways, but enhances NF-Kappa-B and JUN N-terminal kinase dependent signaling through the production of reactive oxygen species (PubMed:18219313).[1] [2] Publication Abstract from PubMedMitochondrial NLRX1 is a member of the family of nucleotide-binding domain and leucine-rich-repeat-containing proteins (NLRs) that mediate host innate immunity as intracellular surveillance sensors against common molecular patterns of invading pathogens. NLRX1 functions in antiviral immunity, but the molecular mechanism of its ligand-induced activation is largely unknown. The crystal structure of the C-terminal fragment (residues 629-975) of human NLRX1 (cNLRX1) at 2.65 A resolution reveals that cNLRX1 consists of an N-terminal helical (LRRNT) domain, central leucine-rich repeat modules (LRRM), and a C-terminal three-helix bundle (LRRCT). cNLRX1 assembles into a compact hexameric architecture that is stabilized by intersubunit and interdomain interactions of LRRNT and LRRCT in the trimer and dimer components of the hexamer, respectively. Furthermore, we find that cNLRX1 interacts directly with RNA and supports a role for NLRX1 in recognition of intracellular viral RNA in antiviral immunity. Structure and Functional Characterization of the RNA-Binding Element of the NLRX1 Innate Immune Modulator.,Hong M, Yoon SI, Wilson IA Immunity. 2012 Mar 23;36(3):337-47. Epub 2012 Mar 1. PMID:22386589[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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