Andreassen H, Bohr H, Bohr J, Brunak S, Bugge T, Cotterill R M, Jacobsen C, Kusk P, Lautrup B, Petersen S B
Laboratory for Protein Chemistry, University of Copenhagen, Denmark.
J Acquir Immune Defic Syndr (1988). 1990;3(6):615-22.
A neural network computer program, trained to predict secondary structure of proteins by exposing it to matching sets of primary and secondary structures from a database, was used to analyze the human immunodeficiency virus (HIV) proteins p17, gp120, and gp41 from their amino acid sequences. The results are compared to those obtained by the Chou-Fasman analysis. Two alpha-helical sequences corresponding to the putative fusigenic domain and to the transmembrane domain of gp41 could be predicted, as well as a possible binding site between p17 and gp41. On the basis of the secondary structure predictions, a three-dimensional model of p17 was constructed. This model was found to represent a stable conformation by an analysis using an energy-minimization program. The model predicts that p17 is attached to the membrane only by the acylated N-terminus, in analogy with the N-terminus of the gag protein of other retroviruses and also with the src oncogene protein p60src. The intracellular C-terminal part of gp41 may act as a receptor by electrostatic interaction with p17.
一个神经网络计算机程序，通过将其暴露于数据库中匹配的一级和二级结构集来训练以预测蛋白质的二级结构，该程序被用于从氨基酸序列分析人类免疫缺陷病毒（HIV）蛋白p17、gp120和gp41。将结果与通过Chou-Fasman分析获得的结果进行比较。可以预测到与gp41的推定融合结构域和跨膜结构域相对应的两个α-螺旋序列，以及p17和gp41之间的一个可能的结合位点。基于二级结构预测，构建了p17的三维模型。通过使用能量最小化程序的分析发现该模型代表一种稳定构象。该模型预测p17仅通过酰化的N末端附着于膜，这与其他逆转录病毒的gag蛋白的N末端以及src癌基因蛋白p60src类似。gp41的细胞内C末端部分可能通过与p17的静电相互作用充当受体。
