Crystallographic characterization of mouse AIM2 HIN-200 domain bound to a 15bp and an 18bp double-stranded DNA

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-1 beta by caspase-1. The DNA-binding HIN-200 domain of mouse AIM2 bound to a 15bp dsDNA an...

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Published inActa crystallographica. Section F, Structural biology and crystallization communications Vol. 68; no. 9; pp. 1081 - 1084
Main Authors Sung, Min Woo, Watts, Tylan, Li, Pingwei
Format Journal Article
LanguageEnglish
Published 01.09.2012
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Summary: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-1 beta by caspase-1. The DNA-binding HIN-200 domain of mouse AIM2 bound to a 15bp dsDNA and to an 18bp dsDNA was purified and crystallized. The AIM2 HIN-200 domain in complex with the 15bp DNA crystallized in the cubic space group I23 or I213, with unit-cell parameter a = 235.60Aa. The complex of the AIM2 HIN-200 domain and the 18bp DNA crystallized in a similar unit cell. Diffraction data for the two complexes were collected to about 4.0Aa resolution. Mutagenesis and DNA-binding studies suggest that mouse AIM2 uses a similar surface to human AIM2 to recognize DNA.
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ISSN:1744-3091
1744-3091
DOI:10.1107/S174430911203103X