Structure of human immunodeficiency virus type 1 Vpr(34–51) peptide in micelle containing aqueous solution

摘要: Human immunodeficiency virus type 1 protein R (HIV-1 Vpr) promotes nuclear entry of viral nucleic acids in nondividing cells, causes G2 cell cycle arrest and is involved cellular differentiation death. Vpr subcellular localization as variable its functions. It known, that consistent with role transport, localizes to the envelope human cells. Further, a reported ion channel activity clearly dependent on or at membranes. We focused our structural studies secondary structure peptide consisting residues 34–51 HIV-1 Vpr. This part plays an important oligomerization, contributes activity, essential for virion incorporation binding HHR23A, DNA repair. Employing NMR spectroscopy we found this be almost completely α helical presence micelles, well trifluoroethanol containing methanol/chloroform solvent. Our results provide data suggesting contain amphipathic, leucine-zipper-like α helix, which serves basis oligomerization interactions factors