Deciphering complement mechanisms: The contributions of structural biology

被引:27
作者
Arlaud, Gerard J.
Barlow, Paul N.
Gaboriaud, Christine
Gros, Piet
Narayana, Sthanam V. L.
机构
[1] Univ Grenoble 1, CNRS, CEA, Inst Biol Struct Jean Pierre Ebel, F-38027 Grenoble, France
[2] Univ Edinburgh, Sch Biol Sci, Biomol NMR Unit, Edinburgh EH8 9YL, Midlothian, Scotland
[3] Univ Edinburgh, Sch Chem, Biomol NMR Unit, Edinburgh EH8 9YL, Midlothian, Scotland
[4] Univ Utrecht, Fac Sci, Bijvoet Ctr Biomol Res, NL-3508 TC Utrecht, Netherlands
[5] Univ Alabama Birmingham, Sch Optometry, Ctr Biophys Sci & Engn, Birmingham, AL 35233 USA
基金
英国医学研究理事会;
关键词
complement; structures; x-ray crystallography; NMR;
D O I
10.1016/j.molimm.2007.06.147
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. (c) 2007 Elsevier Ltd. All rights reserved.
引用
收藏
页码:3809 / 3822
页数:14
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