View source for 2n00


==NMR Solution structure of AIM2 PYD from Mus musculus==
<StructureSection load='2n00' size='340' side='right'caption='[[2n00]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2n00]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N00 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N00 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2n00 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n00 OCA], [https://pdbe.org/2n00 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n00 RCSB], [https://www.ebi.ac.uk/pdbsum/2n00 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n00 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AIM2_MOUSE AIM2_MOUSE] 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.<ref>PMID:19158676</ref> <ref>PMID:19158675</ref> <ref>PMID:19131592</ref> <ref>PMID:20417169</ref> <ref>PMID:20351693</ref> <ref>PMID:20351692</ref> <ref>PMID:20457908</ref> <ref>PMID:22555457</ref> <ref>PMID:21902795</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The inflammasome is a key component of the innate immune system providing the initial defense against invading organisms. Failure of inflammasome formation is the main reason for many innate and acquired immune diseases. Cytosolic protein absent in melanoma 2 (AIM2) has been reported to play an essential role in double-stranded DNA (dsDNA) sensing and inflammasome formation in response to viruses or bacteria infection. The N-terminal pyrin domain (PYD) of AIM2 interacts with the ASC PYD domain, and then recruits downstream proteins to assemble the AIM2 inflammasome. The molecular mechanisms of PYD mediated signaling remain elusive as limited structural information on PYD family. Herein, we characterized the solution structure of mouse AIM2 PYD domain by NMR spectroscopy, and compared it with the crystal structures of its two human homologues. The comparison shows mAIM2 PYD adopts a unique alpha2-alpha3 helix conformation distinct from its human homologues, but similar to the pyrin domain of human NLRP10/PYNOD, which belongs to another family. In addition, the aggregation of mAIM2 PYD domain, with the increased salt concentration, reveals that both the charge surface and hydrophobic interaction play important roles in the self-association of mAIM2 PYD.

The NMR solution structure of AIM2 PYD domain from Mus musculus reveals a distinct alpha2-alpha3 helix conformation from its human homologues.,Hou X, Niu X Biochem Biophys Res Commun. 2015 May 29;461(2):396-400. doi:, 10.1016/j.bbrc.2015.04.046. Epub 2015 Apr 16. PMID:25888795<ref>PMID:25888795</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Hou X]]
[[Category: Niu X]]