![]() ![]() P49 may serve as a novel tool to analyze the contribution of different components of the caspase chain in the apoptotic response in organisms not related phylogenetically. The high structural homology between P49 and P35 suggests that these molecules bear a scaffold common to baculovirus & amp amp amp amp amp amp amp amp amp amp amp quot apoptotic suppressor& amp amp amp amp amp amp amp amp amp amp amp quot proteins. alpha-Helical motifs alpha(1), alpha(2), and alpha(4& amp amp amp amp amp amp amp amp amp amp amp #39 ) were required for P49 function. Our model predicted seven alpha-helical motifs, three of them unique to P49. RSL begins at an amphipathic alpha1 helix, traverses the beta-sheet central region, exposing Asp(94) at the apex, and rejoins the beta-barrel. Finally we identified domains important for P49& amp amp amp amp amp amp amp amp amp amp amp #39 s antiapoptotic function that include a reactive site loop (RSL) protruding from a beta-barrel domain. We demonstrated that P49 is able to inhibit insect and human effector caspases, which requires P49 cleavage at Asp(94). Here we show that sl-p49 encodes a 49-kDa protein, confirmed its primary structure that displays 48.8% identity to P35, and performed computer-assisted modeling of P49 based on the structure of P35. Recently, we have identified sl-p49, a novel apoptosis suppressor gene and the first homologue of p35, in the genome of the Spodoptera littoralis nucleopolyhedrovirus. iap homologues were identified in insects and mammals. P35 is a 35-kDa protein that can suppress apoptosis induced by virus infection or by diverse stimuli in vertebrates or invertebrates. Two antiapoptotic types of genes, iap and p35, were found in baculoviruses.
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