Decroly E, Cornet B, Martin I, Ruysschaert J M, Vandenbranden M
Laboratoire de Chimie-Physique des Macromolécules aux Interfaces, Université Libre de Bruxelles, Belgium.
J Virol. 1993 Jun;67(6):3552-60. doi: 10.1128/JVI.67.6.3552-3560.1993.
The secondary structure of the precursor (gp160) of the envelope protein of human immunodeficiency virus type 1 (BH10) and its receptor-binding subunit (gp120) was studied by Fourier-transformed attenuated total reflection spectroscopy. A higher alpha-helix/beta-sheet ratio in the gp120 subunit than in the precursor indicates a structural heterogeneity between the two subunits (gp120 and gp41), in agreement with classical secondary-structure predictions. The secondary structure of gp41 was estimated and compared with existing models. The high alpha-helical content in gp41 and the dominant beta-sheet content in gp120 resemble the distribution in influenza virus hemagglutinin subunits.
利用傅里叶变换衰减全反射光谱法研究了1型人类免疫缺陷病毒(BH10)包膜蛋白前体(gp160)及其受体结合亚基(gp120)的二级结构。与经典二级结构预测结果一致,gp120亚基中的α-螺旋/β-折叠比例高于前体,这表明两个亚基(gp120和gp41)之间存在结构异质性。对gp41的二级结构进行了估算,并与现有模型进行了比较。gp41中高含量的α-螺旋和gp120中占主导地位的β-折叠含量类似于流感病毒血凝素亚基中的分布。