[Conformation analysis of the N-glycosylation site Asn-X-Thr/Ser in glycoproteins].
Theoretical conformational analysis of oligopeptides CH3CO-Asn-X-Thr-NHCH3 (X = Gly, Ala, Pro), modelling N-glycosylation site, and their glycosylated derivatives CH3CO-(GlcNAc beta 1-4GlcNAc beta 1) Asn-X-Thr-NHCH3 has been carried out. Active conformations of the site are found, corresponding to structural prerequisities of N-glycosylation: Asn residue's position in beta-turn and hydrogen bond formation between side chains of Asn and Thr/Ser residues. In this case the L conformation of the central residue X is most probable. Since Pro residue does not possess this conformation, sequences with X = Pro are not glycosylated. It is shown that glycosylation of the above-mentioned sites is accompanied by reorientation of the Asn residue's side chains.
Avanov
A Ia
AIa
Lipkind
G M
GM
D000595:Amino Acid Sequence; D001216:Asparagine; D006017:Glycolipids / Q000032:analysis; D006023:Glycoproteins / Q000032:analysis*; D006031:Glycosylation; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012694:Serine; D013912:Threonine
D006017:Glycolipids; D006023:Glycoproteins; D013912:Threonine; D012694:Serine; D001216:Asparagine
Konformatsionnyĭ analiz saĭta N-glikozilirovaniia Asn-X-Thr/Ser v glikoproteinakh.