Mechanism of XIAP-Mediated Inhibition of Caspase-9
作者： Eric N Shiozaki , Jijie Chai , Daniel J Rigotti , Stefan J Riedl , Pingwei Li
DOI: 10.1016/S1097-2765(03)00054-6
关键词: Biochemistry 、 Enzyme activator 、 Biology 、 Apoptosis 、 XIAP 、 Recombinant DNA 、 Protein structure 、 Caspase-9 、 Inhibitor of apoptosis 、 Cell biology 、 Caspase
摘要: The inhibitor of apoptosis (IAP) proteins potently inhibit the catalytic activity caspases. While profound insight into inhibition effector caspases has been gained in recent years, mechanism how initiator caspase-9 is regulated by IAPs remains enigmatic. This paper reports crystal structure an inhibitory complex with third baculoviral IAP repeat (BIR3) XIAP at 2.4 A resolution. reveals that BIR3 domain forms a heterodimer monomer. Strikingly, surface interacts also mediates its homodimerization. We demonstrate monomeric catalytically inactive due to absence supporting sequence element could be provided Thus, sequesters state, which serves prevent activity. These studies, conjunction other observations, define unified for activation all
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