Rowlands D, Logan D, Abu-Ghazaleh R, Blakemore W, Curry S, Jackson T, King A, Lea S, Lewis R, Newman J
Laboratory of Molecular Biophysics, University of Oxford.
Arch Virol Suppl. 1994;9:51-8. doi: 10.1007/978-3-7091-9326-6_6.
Residues 136-159 of VPI of foot and mouth disease virus (FMDV) comprise the G-H loop of the protein and form a prominent feature on the surface of virus particles. This sequence contains an immunodominant neutralizing epitope, which can be mimicked with synthetic peptides, and includes an Arg, Gly, Asp motif which has been implicated in the binding of the virus to cellular receptors. Crystallographic analysis of native virus particles failed to resolve the structure of this region due to its disordered state. However, reduction of a disulphide bond between cysteine residues 134 of VP1 and 130 of VP2 caused the G-H loop to collapse onto the surface of the virus particle and allowed its conformation to be determined.
口蹄疫病毒（FMDV）VP1蛋白的136 - 159位氨基酸残基构成了该蛋白的G - H环，在病毒粒子表面形成一个显著特征。该序列包含一个免疫显性中和表位，可用合成肽模拟，还包括一个与病毒和细胞受体结合有关的精氨酸 - 甘氨酸 - 天冬氨酸基序。由于该区域处于无序状态，天然病毒粒子的晶体学分析未能解析其结构。然而，VP1的134位半胱氨酸残基与VP2的130位半胱氨酸残基之间的二硫键还原后，G - H环折叠到病毒粒子表面，从而确定了其构象。
