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

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.

SUBMITTER: Barlow PN

PROVIDER: S-EPMC4863441 | biostudies-literature | 2008

REPOSITORIES: biostudies-literature

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

Barlow Paul N PN Hageman Gregory S GS Lea Susan M SM

Advances in experimental medicine and biology 20080101

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 ...[more]

PMID: 19025119

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