Structure and interdomain dynamics of apoptosis-associated speck-like protein containing a CARD (ASC).

ABSTRACT: The human protein ASC is a key mediator in apoptosis and inflammation. Through its two death domains (pyrin and CARD) ASC interacts with cell death executioners, acts as an essential adapter for inflammasome integrity, and oligomerizes into functional supramolecular assemblies. However, these functions are not understood at the structural-dynamic level. This study reports the solution structure and interdomain dynamics of full-length ASC. The pyrin and CARD domains are structurally independent six-helix bundle motifs connected by a 23-residue linker. The CARD structure reveals two distinctive characteristics; helix 1 is not fragmented as in all other known CARDs, and its electrostatic surface shows a uniform distribution of positive and negative charges, whereas these are commonly separate

SUBMITTER: de Alba E 

PROVIDER: S-EPMC2781708 | biostudies-literature | 2009 Nov

REPOSITORIES: biostudies-literature