Complement factor H: using atomic resolution structure to illuminate disease mechanisms.
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.
Barlow
Paul N
PN
School of Chemistry and Biological Sciences, Joseph Black Chemistry Building, University of Edinburgh, Edinburgh EH9 2PB, UK. Paul.Barlow@ed.ac.uk
Hageman
Gregory S
GS
Lea
Susan M
SM
D001665:Binding Sites / Q000276:immunology; D017242:Complement Factor H / Q000737:chemistry* / Q000235:genetics / Q000276:immunology*; D018360:Crystallography, X-Ray; D015432:Glomerulonephritis, Membranoproliferative / Q000276:immunology*; D006463:Hemolytic-Uremic Syndrome / Q000276:immunology*; D006801:Humans; D008268:Macular Degeneration / Q000276:immunology*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000276:immunology; D053838:Scattering, Small Angle; D055672:Static Electricity; D014461:Ultracentrifugation; D014961:X-Ray Diffraction
D011994:Recombinant Proteins; D017242:Complement Factor H