So far, a variety of apoptosis inhibitory molecules have been found, including P35, CrmA, IAPs, FLIPs and Bcl-2 family of apoptosis inhibitory molecules.
1) P35 and CrmA are broad-spectrum inhibitors of apoptosis. The results of in vitro studies indicate that P35 forms a stable steric hindrance complex with the target molecule through competitive binding and inhibits Caspases activity, while P35 is at the site DMQD! G is specifically cleaved by the target Caspases, and the cleaved P35 has a stronger binding to caspase. CrmA (Cytokine response modfer A) is a serum protease inhibitor that can directly inhibit the activity of various proteases, but it has not been found in mammals Homologous molecule of P35 and CrmA.
2) FLIPs (FLICE-imhibirory proterins) can inhibit Fas / TNFR1-mediated apoptosis. It has many variants, but its N-terminal functional domain (Prodomain) is exactly the same, and the C-terminal has different lengths. FLIPs bind to FADD and Caspase-8, 10 through the DED functional region, antagonize their interaction, and thus inhibit the recruitment of Caspase 8, 10 to the death receptor complex and their initiation.
3) Inhibitors of Apoptosis Protien (IAPs) are a group of proteins with inhibitory effect on apoptosis, firstly cloned from the baculovirus genome, and found to be able to inhibit the host cell death response caused by virus infection. Its characteristic is a functional area composed of about 20 amino acids, which is necessary for IAPs to inhibit apoptosis. They mainly inhibit Caspase3, -7, but do not bind to its zymogen. Combined with zymogen to inhibit apoptosis.
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