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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >The structure of the BIR3 domain of cIAP1 in complex with the N-terminal peptides of SMAC and caspase-9.
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The structure of the BIR3 domain of cIAP1 in complex with the N-terminal peptides of SMAC and caspase-9.

机译：的cIAP1 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. The mechanism of suppression of apoptosis by cIAP1 is less clear. The structure of the BIR3 domain of cIAP1 (cIAP1-BIR3) in complex with N-terminal peptides from both SMAC and caspase-9 has been determined. The binding constants of these peptides to cIAP1-BIR3 have also been determined using the surface plasmon resonance technique. The structures show that the peptides interact with cIAP1 in the same way that they interact with XIAP: both peptides bind in a similar shallow groove in the BIR3 surface, anchored at the N-terminus by a charge-stabilized hydrogen bond. The binding data show that the SMAC and caspase-9 peptides bind with comparable affinities (85 and 48 nM, respectively).
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 caspase-9通过结合;热点的交互的氨基端残留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。抑制细胞凋亡的cIAP1尚不明朗。cIAP1 BIR3域的结构(cIAP1-BIR3)与氨基肽在复杂SMAC和caspase-9已经确定。这些肽的结合常数cIAP1-BIR3也已经决定使用表面等离子体共振技术。结构表明,肽与互动cIAP1以同样的方式相互作用XIAP:肽结合在一个相似的浅BIR3槽的表面,固定n端charge-stabilized氢键。绑定数据显示,SMAC caspase-9肽结合比较紧密联系(85分别为48海里)。

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