3rn2: Difference between revisions

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 ==Structural Basis of Cytosolic DNA Recognition by Innate Immune Receptors==
-<StructureSection load='3rn2' size='340' side='right' caption='[[3rn2]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
+<StructureSection load='3rn2' size='340' side='right'caption='[[3rn2]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3rn2]] is a 4 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=3RN2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RN2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3rn2]] is a 4 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=3RN2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RN2 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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]] 2.55&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3rlo|3rlo]], [[3rln|3rln]], [[3rn5|3rn5]], [[3rnu|3rnu]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AIM2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3rn2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rn2 OCA], [https://pdbe.org/3rn2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rn2 RCSB], [https://www.ebi.ac.uk/pdbsum/3rn2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rn2 ProSAT]</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=3rn2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rn2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rn2 RCSB], [http://www.ebi.ac.uk/pdbsum/3rn2 PDBsum]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/AIM2_HUMAN AIM2_HUMAN] Involved in innate immune response by recognizing cytosolic double-stranded DNA and inducing caspase-1-activating inflammasome formation in macrophages. Upon binding to DNA is thought to undergo oligomerization and to associate with PYCARD initiating the recruitment of caspase-1 precusrsor and processing of interleukin-1 beta and interleukin-18. Detects cytosolic dsDNA of viral and bacterial origin in a non-sequence-specific manner. Can also trigger PYCARD-dependent, caspase-1-independent cell death that involves caspase-8 (By similarity). Tumor suppressor which may act by repressing NF-kappa-B transcriptional activity.<ref>PMID:16432157</ref> <ref>PMID:17726700</ref> <ref>PMID:19158679</ref> <ref>PMID:19158676</ref> <ref>PMID:19158675</ref> <ref>PMID:20566831</ref>
-Recognition of DNA by the innate immune system is central to antiviral and antibacterial defenses, as well as an important contributor to autoimmune diseases involving self DNA. AIM2 (absent in melanoma 2) and IFI16 (interferon-inducible protein 16) have been identified as DNA receptors that induce inflammasome formation and interferon production, respectively. Here we present the crystal structures of their HIN domains in complex with double-stranded (ds) DNA. Non-sequence-specific DNA recognition is accomplished through electrostatic attraction between the positively charged HIN domain residues and the dsDNA sugar-phosphate backbone. An intramolecular complex of the AIM2 Pyrin and HIN domains in an autoinhibited state is liberated by DNA binding, which may facilitate the assembly of inflammasomes along the DNA staircase. These findings provide mechanistic insights into dsDNA as the activation trigger and oligomerization platform for the assembly of large innate signaling complexes such as the inflammasomes.
-Structures of the HIN Domain:DNA Complexes Reveal Ligand Binding and Activation Mechanisms of the AIM2 Inflammasome and IFI16 Receptor.,Jin T, Perry A, Jiang J, Smith P, Curry JA, Unterholzner L, Jiang Z, Horvath G, Rathinam VA, Johnstone RW, Hornung V, Latz E, Bowie AG, Fitzgerald KA, Xiao TS Immunity. 2012 Apr 20;36(4):561-71. Epub 2012 Apr 5. PMID:22483801<ref>PMID:22483801</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
 == References ==
 <references/>
@@ Line 21: / Line 15: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Jin, T C]]
+[[Category: Large Structures]]
-[[Category: Xiao, T]]
+[[Category: Jin TC]]
-[[Category: Cytosolic]]
+[[Category: Xiao T]]
-[[Category: Cytosolic dna sensor]]
-[[Category: Dna binding]]
-[[Category: Immune system-dna complex]]
-[[Category: Inflammasome]]