Similar to other<unk> s,<unk>  has three domains: N-terminal pro-domain, large subunit, and a small subunit. The N-terminal pro-domain is also called the long pro-domain and this contains the<unk>  activation domain (CARD) motif. The pro-domain is linked to the catalytic domain by a linker loop. The<unk>  monomer consists of one large and one small subunit, both comprising the catalytic domain. Differing from the normally conserved active site motif QACRG in other<unk> s,<unk>  has the motif QACGG. When dimerized,<unk>  has two different active site conformations within each dimer. One site closely resembles the catalytic site of other<unk> s, whereas the second has no 'activation loop', disrupting the catalytic machinery in that particular active site. Surface loops around the active site are short, giving rise to broad substrate specificity as the substrate-binding cleft is more open. Within<unk> 's active site, in order for catalytic activity to occur there has to be specific amino acids in the right position. Amino acid Asp at position P1 is essential, with a preference for amino acid His at position P2.
Caspase-9
STAT protein
NLRP3
Bcl-xL
Zinc transporter 8
Fc receptor
IKK2
Thromboxane receptor