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Complement Factor H has recently come to the fore with variant forms implicated in a range of serious disease states. This review aims to bring together recent data concerning the structure and biological activity of this molecule to highlight the way in which a molecular understanding of function may open novel therapeutic possibilities. In particular we examine the evidence for and against the hypothesis that sequence variations in factor H may predispose to disease if they perturb its ability to recognise and respond appropriately to polyanionic carbohydrates on host surfaces that require protection from complement-mediated damage.


Conference paper

Publication Date





117 - 142


Binding Sites, Complement Factor H, Crystallography, X-Ray, Glomerulonephritis, Membranoproliferative, Hemolytic-Uremic Syndrome, Humans, Macular Degeneration, Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Protein Conformation, Protein Structure, Secondary, Protein Structure, Tertiary, Recombinant Proteins, Scattering, Small Angle, Static Electricity, Ultracentrifugation, X-Ray Diffraction