Chaohong Sun

TL;DR: The crystal structure of the second BIR domain of XIAP (BIR2) in complex with caspase-3, at a resolution of 2.7 A, is reported, revealing the structural basis for inhibition and the mechanism of inhibition is due to a steric blockade prohibitive of substrate binding.

TL;DR: The solution structure of the BIR3 domain of X-linked IAP (XIAP) complexed with a functionally active nine-residue peptide derived from the N terminus of Smac is determined and should aid in the design of small molecules that may be used for the treatment of cancers that overexpress IAPs.

TL;DR: The results demonstrate the feasibility of using small molecule inhibitors to selectively target the catalytic activity of histone acetyltransferases, which may provide effective treatments for transcriptional activator-driven malignancies and diseases.

TL;DR: The nuclear magnetic resonance structure of a region encompassing the second BIR domain (BIR2) of a human IAP family member, XIAP (also called hILP or MIHA), is described and it is indicated that conserved amino acids within the linker region between the BIR1 and BIR2 domains were found to be critical for inhibiting caspase-3.

TL;DR: It is shown that the Bir3 domain is the minimal region of XIAP that is needed for potent caspase-9 inhibition, and this results suggest that XIAP inhibits casp enzyme-3 and caspases-9 in a different manner.