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3un9

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Revision as of 07:50, 20 July 2022

Crystal structure of an immune receptor

Structural highlights

3un9 is a 3 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	NLRX1, NOD26, NOD5, NOD9 (HUMAN)
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]

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^[3]

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

References

↑ 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
↑ 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
↑ Hong M, Yoon SI, Wilson IA. Structure and Functional Characterization of the RNA-Binding Element of the NLRX1 Innate Immune Modulator. Immunity. 2012 Mar 23;36(3):337-47. Epub 2012 Mar 1. PMID:22386589 doi:10.1016/j.immuni.2011.12.018

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3un9"

@@ Line 1: / Line 1: @@
 ==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 ==
-<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/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 [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='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='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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NLRX1, NOD26, NOD5, NOD9 ([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'>[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>
 == 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 ==
@@ Line 24: / Line 24: @@
 </StructureSection>
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Hong, M]]
 [[Category: Wilson, I A]]

3un9

From Proteopedia

Revision as of 07:50, 20 July 2022

Crystal structure of an immune receptor

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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