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Article

Structure of complement factor H carboxyl-terminus reveals molecular basis of atypical haemolytic uremic syndrome.

The EMBO journal - 19 Apr 2006

Jokiranta T Sakari, Jaakola Veli-Pekka, Lehtinen Markus J, Pärepalo Maria, Meri Seppo, Goldman Adrian

Abstract excerpt

Factor H (FH) is the key regulator of the alternative pathway of complement. The carboxyl-terminal domains 19-20 of FH interact with the major opsonin C3b, glycosaminoglycans, and endothelial cells. Mutations within this area are associated with atypical haemolytic uremic syndrome (aHUS), a disease characterized by damage to endothelial cells, erythrocytes, and kidney glomeruli. The structure of recombinant...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 16601698
DOI: 10.1038/sj.emboj.7601052
PMCID: PMC1440827

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Structure of complement factor H carboxyl-terminus reveals molecular basis of atypical haemolytic uremic syndrome.PMID 16601698Read ↗

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The binding of factor H to a complex of physiological polyanions and C3b on cells is impaired in atypical hemolytic uremic syndrome.Semantic proximity Read ↗

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Structural Analysis of the C-Terminal Region (Modules 18–20) of Complement Regulator Factor H (FH)Semantic proximity Read ↗

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Antibody recognition of complement factor H reveals a flexible loop involved in atypical hemolytic uremic syndrome pathogenesis.Semantic proximity Read ↗

Dual interaction of factor H with C3d and glycosaminoglycans in host–nonhost discrimination by complementSemantic proximity Read ↗

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