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==Crystal structure of an immune receptor==
==Crystal structure of an immune receptor==
<StructureSection load='3un9' size='340' side='right' caption='[[3un9]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
<StructureSection load='3un9' size='340' side='right'caption='[[3un9]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3un9]] is a 3 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=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 [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3UN9 FirstGlance]. <br>
</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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.65&#8491;</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 HUMAN])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PT:PLATINUM+(II)+ION'>PT</scene></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://pdbe.org/3un9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3un9 RCSB], [http://www.ebi.ac.uk/pdbsum/3un9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3un9 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=3un9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3un9 OCA], [https://pdbe.org/3un9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3un9 RCSB], [https://www.ebi.ac.uk/pdbsum/3un9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3un9 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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> 
[https://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;">
== Publication Abstract from PubMed ==
Mitochondrial 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<ref>PMID:22386589</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3un9" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Hong, M]]
[[Category: Large Structures]]
[[Category: Wilson, I A]]
[[Category: Hong M]]
[[Category: Yoon, S I]]
[[Category: Wilson IA]]
[[Category: Antiviral signaling]]
[[Category: Yoon SI]]
[[Category: Ikk]]
[[Category: Immune system]]
[[Category: Mav]]
[[Category: Traf6]]
[[Category: Uqcrc2]]

Latest revision as of 13:25, 1 March 2024

Crystal structure of an immune receptorCrystal structure of an immune receptor

Structural highlights

3un9 is a 3 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 2.65Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

References

  1. ↑ Tattoli I, Carneiro LA, Jehanno M, Magalhaes JG, Shu Y, Philpott DJ, Arnoult D, Girardin SE. NLRX1 is a mitochondrial NOD-like receptor that amplifies NF-kappaB and JNK pathways by inducing reactive oxygen species production. EMBO Rep. 2008 Mar;9(3):293-300. doi: 10.1038/sj.embor.7401161. Epub 2008 Jan 25. PMID:18219313 doi:http://dx.doi.org/10.1038/sj.embor.7401161
  2. ↑ Moore CB, Bergstralh DT, Duncan JA, Lei Y, Morrison TE, Zimmermann AG, Accavitti-Loper MA, Madden VJ, Sun L, Ye Z, Lich JD, Heise MT, Chen Z, Ting JP. NLRX1 is a regulator of mitochondrial antiviral immunity. Nature. 2008 Jan 31;451(7178):573-7. Epub 2008 Jan 16. PMID:18200010 doi:http://dx.doi.org/nature06501

3un9, resolution 2.65Å

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