Structure and activation of the C1 complex of complement: unraveling the puzzle

被引:203
作者
Gaboriaud, C
Thielens, NM
Gregory, LA
Rossi, V
Fontecilla-Camps, JC
Arlaud, GJ
机构
[1] Univ Grenoble 1, Cristallog & Cristallogenese Prot Lab, F-38027 Grenoble 1, France
[2] Univ Grenoble 1, Lab Enzymol Mol, F-38027 Grenoble 1, France
[3] Univ Grenoble 1, Inst Biol Struct Jean Pierre Ebel, CNRS, CEA, F-38027 Grenoble 1, France
关键词
D O I
10.1016/j.it.2004.04.008
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
C1, the multimolecular protease that triggers the classical pathway of complement, has a major role in the host defense against pathogens. It also participates in other biological functions, such as immune tolerance, owing to the ability of its binding subunit, C1q, to recognize abnormal structures from self, including apoptotic cells. Structural biology has been used over the past few years to elucidate the structure of its three subunits: C1q, C1r and C1s. These new advances have led to a comprehensive, three-dimensional model of C1 and provide insights into the mechanisms underlying its activation and the extraordinarily versatile recognition properties of its C1q subunit.
引用
收藏
页码:368 / 373
页数:6
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