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

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-1 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 . 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 resolution. Mutagenesis and DNA-binding studies suggest that mouse AIM2 uses a similar surface to human AIM2 to recognize DNA.

published proceedings

  • Acta Crystallogr Sect F Struct Biol Cryst Commun

author list (cited authors)

  • Sung, M. W., Watts, T., & Li, P.

citation count

  • 7

complete list of authors

  • Sung, Min Woo||Watts, Tylan||Li, Pingwei

publication date

  • September 2012