Deciphering complement mechanisms: the contributions of structural biology.
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.
Arlaud
Gérard J
GJ
Institut de Biologie Structurale Jean-Pierre Ebel, CEA, CNRS, Université Joseph Fourier, 41 rue Jules Horowitz, F-38027 Grenoble, France. arlaud@ibs.fr
Barlow
Paul N
PN
Gaboriaud
Christine
C
Gros
Piet
P
Narayana
Sthanam V L
SV
D000818:Animals; D020134:Catalytic Domain; D003165:Complement System Proteins / Q000737:chemistry* / Q000276:immunology*; D018360:Crystallography, X-Ray; D006801:Humans; D012697:Serine Endopeptidases / Q000737:chemistry / Q000378:metabolism; D013329:Structure-Activity Relationship
D003165:Complement System Proteins; D012697:Serine Endopeptidases