作者: Jennifer D Watkins , Grant R Campbell , Hubert Halimi , Erwann P Loret
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摘要: Background: The HIV-1 Tat protein is a promising target to develop AIDS therapies, particularly vaccines, due its extracellular role that protects HIV-1-infected cells from the immune system. exists in two different lengths, 86 or 87 residues and 99 101 residues, with long form being predominant clinical isolates. We report here structural study of residue Eli variant using 2D liquid-state NMR, molecular modeling circular dichroism. Results: was obtained solid-phase peptide synthesis purified proven biologically active trans-activation assay. Circular dichroism spectra at temperatures up 70°C showed not random coil 20°C. Homonuclear 1H NMR allowed us identify 1639 distance constraints out which 264 were interresidual. Molecular satisfying least 1474 revealed same folding for model structures. has core region composed part N-terminus including highly conserved Trp 11. extra C-terminus protrude groove between basic cysteine-rich are well exposed solvent. Conclusion: show variants share similar pattern whatever their size, but mutations induce local changes.