首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >The structure of the BIR3 domain of clAP1 in complex with the N-terminal peptides of SMAC and caspase-9
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The structure of the BIR3 domain of clAP1 in complex with the N-terminal peptides of SMAC and caspase-9

机译:的clAP1 BIR3域的结构复杂的氨基肽的SMAC和caspase-9

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摘要

The inhibitor of apoptosis protein (IAP) family of molecules inhibit apoptosis through the suppression of caspase activity. It is known that the XIAP protein regulates both caspase-3 and caspase-9 through direct protein-protein interactions. Specifically, the BIR3 domain of XIAP binds to caspase-9 via a 'hotspot' interaction in which the N-terminal residues of caspase-9 bind in a shallow groove on the surface of XIAP. This interaction is regulated via SMAC, the N-terminus of which binds in the same groove, thus displacing caspase-9.
机译:细胞凋亡蛋白的抑制剂(IAP)的家庭抑制细胞凋亡的分子半胱天冬酶活动的抑制。XIAP蛋白调节caspase-3和caspase-9通过直接蛋白质交互。XIAP结合caspase-9通过一个“热点”交互的氨基端残留caspase-9绑定在一个浅槽表面上XIAP。的n端结合在同一沟,从而取代caspase-9。

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