TAILIEUCHUNG - Báo cáo Y học: Structure of human immunodeficiency virus type 1 Vpr(34–51) peptide in micelle containing aqueous solution

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 in cellular differentiation and cell death. Vpr subcellular localization is as variable as its functions. It is known, that consistent with its role in nuclear transport, Vpr localizes to the nuclear envelope of human cells. Further, a reported ion channel activity of Vpr is clearly dependent on its localization in or at membranes. We focused our structural studies on the secondary structure of a peptide consisting of residues 34–51 of HIV-1 Vpr. This. | Eur. J. Biochem. 269 3264-3269 2002 FEBS 2002 doi Structure of human immunodeficiency virus type 1 Vpr 34-51 peptide in micelle containing aqueous solution Andrea Engler1 Thomas Stangler2 3 and Dieter Willbold3 4 1Lehrstuhl fur Biopolymere Universitat Bayreuth Germany 2Institut fur Molekulare Biotechnologie Jena Germany 3Institut fur Physikalische Biologie Heinrich-Heine-Universitat Dusseldorf Germany 4Forschungszentrum Julich IBI-2 Germany 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 in cellular differentiation and cell death. Vpr subcellular localization is as variable as its functions. It is known that consistent with its role in nuclear transport Vpr localizes to the nuclear envelope of human cells. Further a reported ion channel activity of Vpr is clearly dependent on its localization in or at membranes. We focused our structural studies on the secondary structure of a peptide consisting of residues 34-51 of HIV-1 Vpr. This part of Vpr plays an important role in Vpr oligomerization contributes to cell cycle arrest activity and is essential for virion incorporation and binding to HHR23A a protein involved in DNA repair. Employing NMR spectroscopy we found this part of Vpr to be almost completely a helical in the presence of micelles as well as in trifluoroethanol containing and methanol chloroform solvent. Our results provide structural data suggesting residues 34-51 of Vpr to contain an amphipathic leucine-zipper-like a helix which serves as a basis for oligomerization of Vpr and its interactions with cellular and viral factors involved in subcellular localization and virion incorporation of Vpr. Keywords HIV-1 Vpr solution structure dodecylphosphocholine micelles NMR. Human immunodeficiency virus type 1 HIV-1 is a member of the lentivirus family. In addition to the gag pol and env genes present in all .

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