Conformational analysis of the amino termini (5 residues) of human glycophorin AM and AN: differentiation of the structural features of the TN and T antigenic determinants in relation to their specificity.
The N-terminus of glycophorin A, the main transmembrane erythrocyte glycoprotein responsible for the MN blood-group specificity, has been modelled. As the minimum size of the protein recognised by the antiglycophorin A antibodies is the N-terminal glycopentapeptide, attention was focused on the TN and T antigenic determinants of this size in order to determine wether differences in 3D structure exist and how a specific response with different antibodies is induced.
Pèpe
G
G
Centre de Recherche sur les Mécanismes de la Croissance Cristalline, Universités d'Aix-Marseille II et III, France.
Siri
D
D
Oddon
Y
Y
Pavia
A A
AA
Reboul
J P
JP
D000595:Amino Acid Sequence; D002236:Carbohydrate Conformation; D000939:Epitopes / Q000737:chemistry; D006021:Glycophorins / Q000737:chemistry* / Q000276:immunology; D006801:Humans; D007120:Immunochemistry; D008951:MNSs Blood-Group System / Q000276:immunology; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010446:Peptide Fragments / Q000737:chemistry / Q000276:immunology; D011487:Protein Conformation
D000939:Epitopes; D006021:Glycophorins; D008951:MNSs Blood-Group System; D010446:Peptide Fragments