Complete primary structure and functional characterization of the sixth component of the human complement system. Identification of the C5b-binding domain in complement C6.

Détails

ID Serval
serval:BIB_2ACAB35DEF6C
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Complete primary structure and functional characterization of the sixth component of the human complement system. Identification of the C5b-binding domain in complement C6.
Périodique
Journal of Biological Chemistry
Auteur⸱e⸱s
Haefliger J.A., Tschopp J., Vial N., Jenne D.E.
ISSN
0021-9258
Statut éditorial
Publié
Date de publication
10/1989
Peer-reviewed
Oui
Volume
264
Numéro
30
Pages
18041-18051
Langue
anglais
Notes
Publication types: Comparative Study ; Journal Article
Résumé
Complement C6 is one of five plasma proteins that are incorporated into the lytic terminal complement complex on lipid membranes (C5b-9m) upon activation of the complement cascade. Oligonucleotide probes derived from partial amino acid sequences of purified C6 were used to isolate cDNA clones from a human liver cDNA library. The complete polypeptide structure of mature C6 deduced from the cDNA sequence consists of 913 amino acid residues preceded by a typical 21-residue signal peptide. C6 is most similar in structure to complement C7, sharing 33.5% identical residues with C7 including all 56 cysteine residues. The low density lipoprotein receptor class A and B modules, the thrombospondin type I module at the carboxyl terminus, and the two short consensus repeat modules are arranged in the same way as in C7. In contrast to C7 and other terminal complement proteins, the thrombospondin type I module at the amino terminus occurs as a tandem repeat in C6. The last tandem repeat at the carboxyl terminus of C6 and C7 has been identified as a new distinct module (factor I module), which is closely related to a segment in the heavy chain of complement control factor I. Binding studies with filter-bound C6 fragments generated by proteolysis showed that the C5b-binding domain of C6 was located in the 34-kDa carboxyl terminal fragment consisting of two short consensus repeats and two factor I modules.
Mots-clé
Amino Acid Sequence, Base Sequence, Binding Sites, Cloning, Molecular, Complement C5/metabolism, Complement C5b, Complement C6/genetics, Complement C6/metabolism, Complement System Proteins/genetics, DNA/genetics, Humans, Introns, Molecular Sequence Data, Restriction Mapping, Sequence Homology, Nucleic Acid
Pubmed
Web of science
Création de la notice
24/01/2008 15:18
Dernière modification de la notice
20/08/2019 13:10
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