Journal article
Analysis of the secondary structure of the human immunodeficiency virus (HIV) proteins p17, gp120, and gp41 by computer modeling based on neural network methods
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.
Language: | English |
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Year: | 1990 |
Pages: | 615-622 |
ISSN: | 23312289 and 08949255 |
Types: | Journal article |
Algorithms Amino Acid Sequence Computer Simulation Gene Products, env Gene Products, gag HIV Antigens HIV Envelope Protein gp120 HIV Envelope Protein gp160 HIV Envelope Protein gp41 HIV-1 Models, Molecular Molecular Sequence Data Protein Conformation Protein Precursors Software Viral Proteins gag Gene Products, Human Immunodeficiency Virus p17 protein, Human Immunodeficiency Virus Type 1