Disease-associated sequence variations congregate in a polyanion recognition patch on human factor H revealed in three-dimensional structure.

@article{Herbert2006DiseaseassociatedSV,
  title={Disease-associated sequence variations congregate in a polyanion recognition patch on human factor H revealed in three-dimensional structure.},
  author={Andrew Herbert and Du{\vs}an Uhr{\'i}n and Malcolm Lyon and Michael K. Pangburn and Paul N. Barlow},
  journal={The Journal of biological chemistry},
  year={2006},
  volume={281 24},
  pages={16512-20}
}
Mutations and polymorphisms in the regulator of complement activation, factor H, have been linked to atypical hemolytic uremic syndrome (aHUS), membranoproliferative glomerulonephritis, and age-related macular degeneration. Many aHUS patients carry mutations in the two C-terminal modules of factor H, which normally confer upon this abundant 155-kDa plasma glycoprotein its ability to selectively bind self-surfaces and prevent them from inappropriately triggering the complement cascade via the… CONTINUE READING

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