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Structure paper

TitleElectrostatic interactions contribute to the folded-back conformation of wild type human factor H.
Journal, issue, pagesJ. Mol. Biol., Vol. 391, Page 98-118, Year 2009
Publish dateFeb 18, 2009 (structure data deposition date)
AuthorsOkemefuna, A.I. / Nan, R. / Gor, J. / Perkins, S.J.
External linksJ. Mol. Biol. / PubMed:19505476
Methodssmall angle scattering
Structure data

PDB-3gau:
Solution structure of Human Complement Factor H in 50 mM NaCl buffer
Method: SOLUTION SCATTERING

PDB-3gav:
Solution structure of Human Complement Factor H in 137 mM NaCl buffer
Method: SOLUTION SCATTERING

PDB-3gaw:
Solution structure of Human Complement Factor H in 250 mM NaCl buffer
Method: SOLUTION SCATTERING

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

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