The Inhibitor of Apoptosis family
The ‘inhibitor of apoptosis’ (IAP) proteins inhibits apoptosis through blocking the action of caspases, a family of cysteine aspartyl proteases that dismantle the cell, and act downstream of the Bcl-2 family. All IAPs contain at least one BIR (baculoviral IAP repeat) domain, a ~70 residue zinc-binding protein-protein interaction domain which we were the first to describe at atomic resolution. IAPs contain multiple BIRs together with a RING (really interesting new gene 1) domain, and some contain caspase recruitment domains. It has been shown recently that these other domains play important roles in regulating the IAPs and we are interested in determining the structures of protein-protein complexes formed by these domains to elucidate their interactions.
Structure of BIR3 domain.