The sequence and topology of human complement component C9
Détails
ID Serval
serval:BIB_2E2611B792AF
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
The sequence and topology of human complement component C9
Périodique
EMBO Journal
ISSN
0261-4189 (Print)
Statut éditorial
Publié
Date de publication
02/1985
Volume
4
Numéro
2
Pages
375-382
Notes
Comparative Study Journal Article Research Support, Non-U.S. Gov't --- Old month value: Feb
Résumé
A partial nucleotide sequence of human complement component C9 cDNA representing 94% of the coding region of the mature protein is presented. The amino acid sequence predicted from the open reading frame of this cDNA concurs with the amino acid sequence at the amino-terminal end of three proteolytic fragments of purified C9 protein. No long stretches of hydrophobic residues are present, even in the carboxy-terminal half of the molecule which reacts with lipid-soluble photoaffinity probes. Monoclonal antibody epitopes have been mapped by comparing overlapping fragments of C9 molecule to which the antibodies bind on Western blots. Several of these epitopes map to small regions containing other surface features (e.g., proteolytic cleavage sites and N-linked oligosaccharide). The amino-terminal half of C9 is rich in cysteine residues and contains a region with a high level of homology to the LDL receptor cysteine-rich domains. A model for C9 topology based on these findings is proposed.
Mots-clé
Amino Acid Sequence Antibodies, Monoclonal/diagnostic use Base Sequence *Complement C9/genetics DNA, Recombinant Humans Peptide Fragments/immunology Protein Conformation Receptors, LDL/genetics
Pubmed
Web of science
Création de la notice
24/01/2008 15:19
Dernière modification de la notice
20/08/2019 13:12