Avanov A Ia, Lipkind G M
Bioorg Khim. 1990 Mar;16(3):309-17.
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.
对模拟N-糖基化位点的寡肽CH3CO-Asn-X-Thr-NHCH3（X = Gly、Ala、Pro）及其糖基化衍生物CH3CO-(GlcNAcβ1-4GlcNAcβ1)Asn-X-Thr-NHCH3进行了理论构象分析。发现了该位点的活性构象，其符合N-糖基化的结构先决条件：Asn残基在β-转角中的位置以及Asn与Thr/Ser残基侧链之间形成氢键。在这种情况下，中心残基X的L构象最有可能。由于Pro残基不具有这种构象，因此X = Pro的序列不会被糖基化。结果表明，上述位点的糖基化伴随着Asn残基侧链的重新定向。
