<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Sung MW</submitter><funding>NCRR NIH HHS</funding><funding>NIAID NIH HHS</funding><pagination>1081-4</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3433203</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>68(Pt 9)</volume><pubmed_abstract>AIM2 (absent in melanoma 2) is an innate immune receptor for cytosolic double-stranded DNA (dsDNA). The engagement of dsDNA by AIM2 activates the AIM2 inflammasome, resulting in the cleavage of pro-interleukin-1β by caspase-1. The DNA-binding HIN-200 domain of mouse AIM2 bound to a 15 bp dsDNA and to an 18 bp dsDNA was purified and crystallized. The AIM2 HIN-200 domain in complex with the 15 bp DNA crystallized in the cubic space group I23 or I2(1)3, with unit-cell parameter a = 235.60 Å. The complex of the AIM2 HIN-200 domain and the 18 bp DNA crystallized in a similar unit cell. Diffraction data for the two complexes were collected to about 4.0 Å resolution. Mutagenesis and DNA-binding studies suggest that mouse AIM2 uses a similar surface to human AIM2 to recognize DNA.</pubmed_abstract><journal>Acta crystallographica. Section F, Structural biology and crystallization communications</journal><pubmed_title>Crystallographic characterization of mouse AIM2 HIN-200 domain bound to a 15 bp and an 18 bp double-stranded DNA.</pubmed_title><pmcid>PMC3433203</pmcid><funding_grant_id>R01 AI087741</funding_grant_id><funding_grant_id>AI087741</funding_grant_id><funding_grant_id>P41 RR001209</funding_grant_id><pubmed_authors>Watts T</pubmed_authors><pubmed_authors>Sung MW</pubmed_authors><pubmed_authors>Li P</pubmed_authors></additional><is_claimable>false</is_claimable><name>Crystallographic characterization of mouse AIM2 HIN-200 domain bound to a 15 bp and an 18 bp double-stranded DNA.</name><description>AIM2 (absent in melanoma 2) is an innate immune receptor for cytosolic double-stranded DNA (dsDNA). The engagement of dsDNA by AIM2 activates the AIM2 inflammasome, resulting in the cleavage of pro-interleukin-1β by caspase-1. The DNA-binding HIN-200 domain of mouse AIM2 bound to a 15 bp dsDNA and to an 18 bp dsDNA was purified and crystallized. The AIM2 HIN-200 domain in complex with the 15 bp DNA crystallized in the cubic space group I23 or I2(1)3, with unit-cell parameter a = 235.60 Å. The complex of the AIM2 HIN-200 domain and the 18 bp DNA crystallized in a similar unit cell. Diffraction data for the two complexes were collected to about 4.0 Å resolution. Mutagenesis and DNA-binding studies suggest that mouse AIM2 uses a similar surface to human AIM2 to recognize DNA.</description><dates><release>2012-01-01T00:00:00Z</release><publication>2012 Sep</publication><modification>2024-11-12T20:20:26.836Z</modification><creation>2019-03-27T00:14:17Z</creation></dates><accession>S-EPMC3433203</accession><cross_references><pubmed>22949200</pubmed><doi>10.1107/s174430911203103x</doi><doi>10.1107/S174430911203103X</doi></cross_references></HashMap>