Arlaud Gérard J, Barlow Paul N, Gaboriaud Christine, Gros Piet, Narayana Sthanam V L
Institut de Biologie Structurale Jean-Pierre Ebel, CEA, CNRS, Université Joseph Fourier, 41 rue Jules Horowitz, F-38027 Grenoble, France.
Mol Immunol. 2007 Sep;44(16):3809-22. doi: 10.1016/j.molimm.2007.06.147.
Since the resolution of the first three-dimensional structure of a complement component in 1980, considerable efforts have been put into the investigation of this system through structural biology techniques, resulting in about a hundred structures deposited in the Protein Data Bank by the beginning of 2007. By revealing its mechanisms at the atomic level, these approaches significantly improve our understanding of complement, opening the way to the rational design of specific inhibitors. This review is co-authored by some of the researchers currently involved in the structural biology of complement and its purpose is to illustrate, through representative examples, how X-ray crystallography and NMR techniques help us decipher the many sophisticated mechanisms that underlie complement functions.
自1980年解析出首个补体成分的三维结构以来，人们通过结构生物学技术对该系统展开了大量研究，到2007年初已有约一百个结构存入蛋白质数据库。通过在原子水平揭示其机制，这些方法显著增进了我们对补体的理解，为合理设计特异性抑制剂开辟了道路。这篇综述由目前参与补体结构生物学研究的一些研究人员共同撰写，其目的是通过代表性实例说明X射线晶体学和核磁共振技术如何帮助我们解读构成补体功能基础的诸多复杂机制。
