Complement factor H: using atomic resolution structure to illuminate disease mechanisms

Adv Exp Med Biol. 2008:632:117-42.

Abstract

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.

Publication types

  • Review

MeSH terms

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

Substances

  • Recombinant Proteins
  • Complement Factor H