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

Paul N Barlow1, Gregory S Hageman, Susan M Lea

  • 1School of Chemistry and Biological Sciences, Joseph Black Chemistry Building, University of Edinburgh, Edinburgh EH9 2PB, UK. Paul.Barlow@ed.ac.uk

Advances in Experimental Medicine and Biology
|November 26, 2008
PubMed

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.

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