Structure of the absent in melanoma 2 (AIM2) pyrin domain provides insights into the mechanisms of AIM2 autoinhibition and inflammasome assembly.

ABSTRACT:

Background

AIM2 binds dsDNA and associates with ASC through their PYDs to form an inflammasome.

Results

The AIM2 PYD structure illustrates distinct charge distribution and a unique hydrophobic patch.

Conclusion

The AIM2 PYD may bind the ASC PYD and the AIM2 HIN domain through overlapping surface.

Significance

These findings provide insights into the mechanisms of AIM2 autoinhibition and inflammasome assembly. Absent in melanoma 2 (AIM2) is a cytosolic double-stranded (dsDNA) sensor essential for innate immune responses against DNA viruses and bacteria such as Francisella and Listeria. Upon dsDNA engagement, the AIM2 amino-terminal pyrin domain (PYD) is responsible for downstream signaling to the adapter protein apoptosis-associated speck-like protein containing

SUBMITTER: Jin T 

PROVIDER: S-EPMC3650362 | biostudies-literature | 2013 May

REPOSITORIES: biostudies-literature