1DSK

NMR SOLUTION STRUCTURE OF VPR59_86, 20 STRUCTURES

Summary for 1DSK

• Entry DOI: 10.2210/pdb1dsk/pdb
• Descriptor: VPR PROTEIN (1 entity in total)
• Functional Keywords: viral peptide, polypeptide
• Biological source: Human immunodeficiency virus 1
• Cellular location: Virion : P12520
• Total number of polymer chains: 1
• Total formula weight: 3353.07

Authors

Yao, S.,Torres, A.M.,Azad, A.A.,Macreadie, I.G.,Norton, R.S. (deposition date: 1997-10-23, release date: 1998-07-01, Last modification date: 2024-04-10)

Primary citation

Yao, S.,Torres, A.M.,Azad, A.A.,Macreadie, I.G.,Norton, R.S.
Solution structure of peptides from HIV-1 Vpr protein that cause membrane permeabilization and growth arrest.
J. Pept. Sci., 4:426-435, 1998

PubMed Abstract: Vpr, one of the accessory gene products encoded by HIV-1, is a 96-residue protein with a number of functions, including targeting of the viral pre-integration complex to the nucleus and inducing growth arrest of dividing cells. We have characterized by 2D NMR the solution conformations of bioactive synthetic peptide fragments of Vpr encompassing a pair of H(F/S)RIG sequence motifs (residues 71-75 and 78-82 of HIV-1 Vpr) that cause cell membrane permeabilization and death in yeast and mammalian cells. Due to limited solubility of the peptides in water, their structures were studied in aqueous trifluoroethanol. Peptide Vpr59-86 (residues 59-86 of Vpr) formed an alpha-helix encompassing residues 60-77, with a kink in the vicinity of residue 62. The first of the repeated sequence motifs (HFRIG) participated in the well-defined alpha-helical domain whereas the second (HSRIG) lay outside the helical domain and formed a reverse turn followed by a less ordered region. On the other hand, peptides Vpr71-82 and Vpr71-96, in which the sequence motifs were located at the N-terminus, were largely unstructured under similar conditions, as judged by their C(alpha)H chemical shifts. Thus, the HFRIG and HSRIG motifs adopt alpha-helical and turn structures, respectively, when preceded by a helical structure, but are largely unstructured in isolation. The implications of these findings for interpretation of the structure-function relationships of synthetic peptides containing these motifs are discussed.

PubMed: 9851370
DOI: 10.1002/(SICI)1099-1387(199811)4:7<426::AID-PSC161>3.0.CO;2-J

Experimental method

SOLUTION NMR