THE MEMBRANE ATTACK COMPLEX OF COMPLEMENT - ASSEMBLY, STRUCTURE AND CYTOTOXIC ACTIVITY
THE MEMBRANE ATTACK COMPLEX OF COMPLEMENT - ASSEMBLY, STRUCTURE AND CYTOTOXIC ACTIVITY
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DOI：
10.1016/0300-483x(94)90253-4
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发表时间：
1994-02-28
期刊：
影响因子：
4.5
通讯作者：
ESSER, AF
中科院分区：
文献类型：
--
作者：
ESSER, AF
补体的膜攻击复合体是由5个末端补体蛋白C5、C6、C7、C8和C9的分子融合形成的。虽然靶膜上的组装过程以及宿主细胞上存在的限制因子对其的调节现在已经很清楚了，但该复合物结构的分子细节仍需要进一步阐明。对于提供复合物细胞毒性作用的最后作用蛋白C9与前体C5b-8复合物的相互作用尤其如此。由于缺乏结构细节，导致补体介导的细胞死亡的分子机制仍然是神秘的，然而，希望通过重组DNA技术控制组装过程和末端补体蛋白的位点特异性修饰的最新进展能够迅速改变这一困境。
The membrane attack complex of complement is formed by the molecular fusion of the five terminal complement proteins, C5, C6, C7, C8, and C9. While the assembly process on a target membrane and its modulation by restriction factors present on host cells is now quite well understood the molecular details of the architecture of the complex still need much further clarification. This is especially true for the interaction of the last acting protein C9, which provides the cytotoxic action of the complex, with the precursor C5b-8 complex. Because of this lack of structural details the molecular mechanisms that lead to complement-mediated cell death remain cryptic, however, it is hoped that recent advances in controlling the assembly process and in site-specific modification of the terminal complement proteins by recombinant DNA techniques should change this predicament quickly.