| Literature DB >> 12440956 |
P F Zipfel1, C Skerka, J Hellwage, S T Jokiranta, S Meri, V Brade, P Kraiczy, M Noris, G Remuzzi.
Abstract
At present, the human Factor H protein family represents seven multidomain, multifunctional serum proteins. This group includes the complement and immune regulators Factor H, the Factor H-like protein 1 (FHL-1) and five Factor H-related proteins proteins (FHR-1, -2, -3, -4 and -5). Each is exclusively composed of individually folded protein domains, termed short consensus repeats (SCRs) or complement control modules. Structure-function analyses allowed the localization of the complement regulatory domain of Factor H and FHL-1 in the N-terminal region within SCRs 1-4. In addition, multiple binding sites for C3b, heparin and microbial surface proteins were localized in the N-terminus, within the middle region and also in the C-terminus of Factor H and FHL-1. Recent results show a central role for the C-terminus of Factor H, i.e. SCRs 19-20. These particular domains are conserved in all FHRs identified so far, include contact points for C3b, heparin and microbial surface proteins and represent a 'hot-spot' for gene mutations in patients that suffer from the Factor H-associated form of haemolytic uraemic syndrome.Entities:
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Year: 2002 PMID: 12440956 DOI: 10.1042/bst0300971
Source DB: PubMed Journal: Biochem Soc Trans ISSN: 0300-5127 Impact factor: 5.407