CONFORMATION OF THE HIV-1 GP 120 V3 LOOP. STRUCTURE FUNCTIONAL ANALYSIS OF THE HIV-HAITI VIRAL STRAIN
A. M. Andrianov
Institute of Bioorganic Chemistry, National Academy of Sciences of Belaus, Minsk, Belarus;
e-mail: andrianov@iboch.bas-net.by
The structural model describing the conformational preferences of the HIV-Haiti gp 120 V3 loop in geometric space
of dihedral angles was generated in terms of NMR spectroscopy data using the methods of computer modeling. The
elements of secondary structure and conformations of irregular stretches were deciphered for the fragment making the
virus principal neutralizing determinant as well as the determinants of cell tropism and syncytium formation. The
structurally conserved amino acids of the HIV-1 V3 loop, that may present the forward-looking targets for AIDS drug
design, were identified based on the combined analysis of the results obtained with those derived previously. In
particular, it was demonstrated that the register of these amino acids comprises Asn-25 critical for virus binding
with primary cell receptor CD4 as well as Arg-3 critical for utilization of CCR5 coreceptor and heparan sulfate
proteoglycan syndecans. The results obtained are discussed in conjunction with the literature data on the biological
activity of individual amino acid residues of the HIV-1 gp120 V3 loop.
Key words: human immunodeficiency virus type 1, protein gp 120, V3 loop, conformation, computer
modeling, NMR spectroscopy
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