Open AccessCrystallographic characterization of mouse AIM2 HIN‐200 domain bound to a 15 bp and an 18 bp double‐stranded DNA
Author(s) -
Sung Min Woo,
Watts Tylan,
Li Pingwei
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430911203103x
Subject(s) - aim2 , dna , inflammasome , microbiology and biotechnology , pyrin domain , chemistry , biology , receptor , biochemistry
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 I 23 or I 2 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.