title: [Structure and conformational properties of the HIV Thailand gp120 immunodominant epitope].
abstract: NMR data and the previously developed theoretical method were used to determine the three-dimensional structure of the immunodominant epitope (IDE) of the HIVThailand. protein gp120. The best energy IDE conformers consistent with the theoretical and experimental data were calculated, and their ensemble was shown to give rise to the main chain folds found earlier in examining the HIVMN IDE structure. The gp120 IDE is supposed to behave as a metastable oligopeptide that, depending on the microenvironment, largely assumes one of the conformations from the ensemble. The results are discussed in the light of literature data on HIV-1 IDE structure.
authors.affiliation: Institute of Bioorganic Chemistry, National Academy of Sciences, Minsk, 220141 Belarus. Lando@iboch.bas-net.by
authors.forename: A M
authors.initials: AM
authors.lastname: Andrianov
mesh_terms: D000939:Epitopes / Q000737:chemistry*; D015699:HIV Envelope Protein gp120 / Q000737:chemistry* / Q000276:immunology; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D010446:Peptide Fragments / Q000737:chemistry; D011487:Protein Conformation; D012996:Solutions; D013785:Thailand
chemical_list: D000939:Epitopes; D015699:HIV Envelope Protein gp120; D010446:Peptide Fragments; D012996:Solutions