Wong N K, Renouf D V, Lehmann S, Hounsell E F
School of Biological & Chemical Sciences, Birkbeck, University of London, United Kingdom.
J Mol Graph Model. 2000 Apr;18(2):126-34, 163-5. doi: 10.1016/S1093-3263(00)00044-9.
The three-dimensional coordinates from a nuclear magnetic resonance (NMR)-averaged structure containing residues 121-226 of mouse prion were used as the starting geometry for MD of prion either with or without glycan in both mutant and wild-type forms. The following mutants were studied: Asp-178 to Asn, Thr-183 to Ala, Phe-198 to Ser, Glu-200 to Lys, and Gln-217 to Arg. NMR data vs structural models were compared to observe any major differences. Simulations of the change in protein structure with and without glycan were performed, as they cannot be tested by NMR analysis. Several mutants were expressed and analyzed for altered glycosylation and the results interpreted in terms of molecular modeling. N-linked glycosylation is likely to play an important role in prion biology as shown by visualization of glycoprotein conformation.
来自包含小鼠朊病毒121 - 226位残基的核磁共振（NMR）平均结构的三维坐标，被用作朊病毒在有或没有聚糖情况下，突变型和野生型形式分子动力学（MD）模拟的起始几何结构。研究了以下突变体：天冬氨酸178突变为天冬酰胺、苏氨酸183突变为丙氨酸、苯丙氨酸198突变为丝氨酸、谷氨酸200突变为赖氨酸、谷氨酰胺217突变为精氨酸。比较了NMR数据与结构模型，以观察任何主要差异。进行了有或没有聚糖情况下蛋白质结构变化的模拟，因为这些无法通过NMR分析进行测试。表达并分析了几种突变体的糖基化改变情况，并根据分子建模对结果进行了解释。如糖蛋白构象可视化所示，N - 连接糖基化可能在朊病毒生物学中起重要作用。
