4lnq: Difference between revisions
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==Crystal structure of Ifi202 HINa domain in complex with 20bp dsDNA== | |||
=== | <StructureSection load='4lnq' size='340' side='right' caption='[[4lnq]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4lnq]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LNQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LNQ FirstGlance]. <br> | |||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ifi202, Ifi202a, Ifi202b ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=4lnq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lnq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lnq RCSB], [http://www.ebi.ac.uk/pdbsum/4lnq PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The HIN-200 family of proteins play significant roles in inflammation-related processes. Among them, AIM2 (absent in melanoma 2) and IFI16 (gamma-interferon-inducible protein 16) recognize double-stranded DNA to initiate inflammatory responses. In contrast, p202, a mouse interferon-inducible protein containing two HIN domains (HINa and HINb), has been reported to inhibit Aim2-mediated inflammatory signalling in mouse. To understand the inhibitory mechanism, the crystal structure of the p202 HINa domain in complex with a 20 bp DNA was determined, in which p202 HINa nonspecifically recognizes both strands of DNA through electrostatic attraction. The p202 HINa domain binds DNA more tightly than does AIM2 HIN, and the DNA-binding mode of p202 HINa is different from that of the AIM2 HIN and IFI16 HINb domains. These results, together with the reported data on p202 HINb, lead to an interaction model for full-length p202 and dsDNA which provides a conceivable mechanism for the negative regulation of Aim2 inflammasome activation by p202. | |||
Structural mechanism of DNA recognition by the p202 HINa domain: insights into the inhibition of Aim2-mediated inflammatory signalling.,Li H, Wang J, Wang J, Cao LS, Wang ZX, Wu JW Acta Crystallogr F Struct Biol Commun. 2014 Jan;70(Pt 1):21-9. doi:, 10.1107/S2053230X1303135X. Epub 2013 Dec 24. PMID:24419611<ref>PMID:24419611</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
== | <references/> | ||
__TOC__ | |||
[[Category: Li, H | </StructureSection> | ||
[[Category: Wang, Z X | [[Category: Lk3 transgenic mice]] | ||
[[Category: Wu, J W | [[Category: Li, H]] | ||
[[Category: Wang, Z X]] | |||
[[Category: Wu, J W]] | |||
[[Category: Dna binding]] | [[Category: Dna binding]] | ||
[[Category: Dna binding protein-dna complex]] | [[Category: Dna binding protein-dna complex]] | ||
[[Category: Ob fold]] | [[Category: Ob fold]] |