A structural feature common to all IAP family proteins is that they all contain at least one baculoviral IAP repeat (BIR) domain characterized by a conserved zinc-coordinating Cys/His motif at the N-terminal half of the protein.<unk>  is distinguished from other IAP family members in that it has only one BIR domain. The mice and human BIR domain of<unk>  are very similar structurally except for two differences that may affect function variability. The human<unk>  also contains an elongated C-terminal helix comprising 42 amino acids.<unk>  is 16.5 kDa large and is the smallest member of the IAP family. X-ray crystallography has shown two molecules of human<unk> g coming together to form a bowtie-shape dimer through a hydrophobic interface. This interface includes N-terminal residues 6-10 just before the BIR domain region and the 10 residue region connecting the BIR domain to the C-terminal helix. The structural integrity of the determined crystal structure of<unk>  is quite reliable, as physiological conditions were used to obtain the images.
Survivin
Tetherin
Perospirone
Adhyperforin
Diamphotoxin
Lectin
Suramin
Visine