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TitleThe regulatory SCR-1/5 and cell surface-binding SCR-16/20 fragments of factor H reveal partially folded-back solution structures and different self-associative properties.
Journal, issue, pagesJ. Mol. Biol., Vol. 375, Page 80-101, Year 2008
Publish dateJun 27, 2007 (structure data deposition date)
AuthorsOkemefuna, A.I. / Gilbert, H.E. / Griggs, K.M. / Ormsby, R.J. / Gordon, D.L. / Perkins, S.J.
External linksJ. Mol. Biol. / PubMed:18005991
Methodssmall angle scattering
Structure data

PDB-2qfg:
Solution Structure of the N-terminal SCR-1/5 fragment of Complement Factor H.
Method: SOLUTION SCATTERING

PDB-2qfh:
Solution Structure of the C-terminal SCR-16/20 fragment of Complement Factor H.
Method: SOLUTION SCATTERING

Source
  • homo sapiens (human)
KeywordsIMMUNE SYSTEM / X-ray scattering / complement / SCR domain / Factor H / Age-related macular degeneration / Complement alternate pathway / Disease mutation / Glycoprotein / Immune response / Innate immunity / Sushi

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