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...

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Bibliographic Details
Published in:Molecular immunology 2007-09, Vol.44 (16), p.3809-3822
Main Authors: Arlaud, Gérard J., Barlow, Paul N., Gaboriaud, Christine, Gros, Piet, Narayana, Sthanam V.L.
Format: Article
Language:English
Subjects:
Animals
Catalytic Domain
Complement
Complement System Proteins - chemistry
Complement System Proteins - immunology
Crystallography, X-Ray
Humans
NMR
Serine Endopeptidases - chemistry
Serine Endopeptidases - metabolism
Structure-Activity Relationship
Structures
X-ray crystallography
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Summary: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.
ISSN:0161-5890
1872-9142
DOI:10.1016/j.molimm.2007.06.147