A PROPOSED MOLECULAR-MODEL FOR THE CARBOXY TERMINUS OF HIV-1 GP120 SHOWING STRUCTURAL FEATURES CONSISTENT WITH THE PRESENCE OF A T-CELL ALLOEPITOPE

A computer graphics molecular model of the C terminus of gp120 of HIV has been constructed using predicted secondary structure based on homologies with proteins for which X-ray crystallographic data have been published. The model shows sequences known to be important in CD4 binding in close proximity to regions with a high probability of forming alpha-helical and beta-strand motifs. The orientation adopted by these domains approximates to the known 3D structure of HLA-A2 alpha-2 chain without constraints based on HLA-A2 as a template being introduced. The model may therefore represent an energetically favourable conformation for a part of gp120 which mimics the binding domain for the T-cell receptor on MHC molecules. Recognition of gp120 as an alloepitope in high affinity association with CD4 would explain many of the sequelae of acquired immune deficiency on HIV infection.