Solution structure of the RAIDD CARD and model for CARD/CARD interaction in caspase-2 and caspase-9 recruitment
Solution structure of the RAIDD CARD and model for CARD/CARD interaction in caspase-2 and caspase-9 recruitment
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DOI：
10.1016/s0092-8674(00)81417-8
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发表时间：
1998-07-24
期刊：
影响因子：
64.5
通讯作者：
Wagner, G
中科院分区：
文献类型：
--
作者：
Chou, JJ;Matsuo, H;Wagner, G
细胞凋亡需要通过衔接蛋白的CARD（半胱天冬酶募集结构域）和半胱天冬酶的前结构域之间的嗜同性相互作用由受体相关衔接子募集半胱天冬酶。我们已经解决了招募ICH-1/caspase-2的RAIDD衔接蛋白的CARD结构。它由六个紧密堆积的螺旋排列在一个拓扑结构同源的Fas死亡结构域。表面包含一个碱性和一个酸性补丁的相对两侧。如同源性建模所示，该极性在ICH-1 CARD中是保守的。突变数据表明，这些斑块介导RAIDD和ICH-1之间的CARD/CARD相互作用。随后对Apaf-1和半胱天冬酶-9以及Ced-4和Ced-3的CARD的建模表明，碱性/酸性表面极性是高度保守的，表明CARD/CARD相互作用的一般模式。
Apoptosis requires recruitment of caspases by receptor-associated adaptors through homophilic interactions between the CARDs (caspase recruitment domains) of adaptor proteins and prodomains of caspases. We have solved the CARD structure of the RAIDD adaptor protein that recruits ICH-1/caspase-2. It consists of six tightly packed helices arranged in a topology homologous to the Fas death domain. The surface contains a basic and an acidic patch on opposite sides. This polarity is conserved in the ICH-1 CARD as indicated by homology modeling. Mutagenesis data suggest that these patches mediate CARD/CARD interaction between RAIDD and ICH-1. Subsequent modeling of the CARDs of Apaf-1 and caspase-9, as well as Ced-4 and Ced-3, showed that the basic/acidic surface polarity is highly conserved, suggesting a general mode for CARD/CARD interaction.