Open AccessStructure of human immunodeficiency virus type 1 Vpr(34–51) peptide in micelle containing aqueous solution
Author(s) -
Engler Andrea,
Stangler Thomas,
Willbold Dieter
Publication year - 2002
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1046/j.1432-1033.2002.03005.x
Subject(s) - subcellular localization , nuclear transport , nuclear localization sequence , microbiology and biotechnology , nucleic acid , gp41 , peptide , nuclear pore , biology , nls , biophysics , dna , leucine zipper , biochemistry , chemistry , cell nucleus , peptide sequence , antibody , nucleus , cytoplasm , epitope , gene , immunology
Human immunodeficiency virus type 1 protein R (HIV‐1 Vpr) promotes nuclear entry of viral nucleic acids in nondividing cells, causes G 2 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 α 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 α 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.