Hom K, Gochin M, Peumans W J, Shine N
Institute of Biomedical Sciences, Academia Sinica, Nankang, Taipei, Taiwan, ROC.
FEBS Lett. 1995 Mar 20;361(2-3):157-61. doi: 10.1016/0014-5793(95)00133-t.
The binding of the trisaccharide, N,N',N"-triacetylchitotriose, to Urtica dioica agglutinin (UDA) was investigated using 1H NMR spectroscopy. UDA is a small antiviral plant lectin containing two homologous 43-amino acid domains. Carbohydrate-induced pertubations occur in one domain of UDA at trisaccharide concentrations below equimolar. Residues in the second domain are shifted at higher carbohydrate concentrations. This data confirms the presence of two binding sites of non-identical affinities per UDA monomer. Qualitative analysis of the 2D NOESY spectra indicates that UDA contains two short stretches of antiparallel beta-sheet. The 1H resonance assignments for both antiparallel beta-sheet sequences have been completed and there is one beta-stretch per domain. A number of these beta-sheet residues are perturbed in the presence of carbohydrate.
利用核磁共振氢谱（1H NMR）研究了三糖N，N'，N''-三乙酰壳三糖与荨麻凝集素（UDA）的结合。UDA是一种小型抗病毒植物凝集素，包含两个同源的43个氨基酸的结构域。在低于等摩尔浓度的三糖条件下，碳水化合物诱导的扰动出现在UDA的一个结构域中。在较高的碳水化合物浓度下，第二个结构域中的残基会发生位移。该数据证实每个UDA单体存在两个亲和力不同的结合位点。二维核Overhauser效应光谱（2D NOESY）的定性分析表明，UDA包含两段短的反平行β-折叠。已完成两个反平行β-折叠序列的1H共振归属，每个结构域有一个β-伸展。在碳水化合物存在的情况下，许多这些β-折叠残基会受到扰动。
