Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1KZT

Structure of Human Immunodeficiency Virus Type 1 Vpr(34-51) Peptide in DPC Micelle Containing Aqueous Solution

Summary for 1KZT
Entry DOI10.2210/pdb1kzt/pdb
Related1kzs 1kzv
NMR InformationBMRB: 5283
DescriptorVpr PROTEIN (1 entity in total)
Functional Keywordshiv-1, vpr, solution structure, dodecylphosphocholine, micelles, viral protein
Cellular locationVirion: P12520
Total number of polymer chains1
Total formula weight2271.58
Authors
Engler, A.,Stangler, T.,Willbold, D. (deposition date: 2002-02-08, release date: 2002-08-28, Last modification date: 2022-02-23)
Primary citationEngler, A.,Stangler, T.,Willbold, D.
Structure of human immunodeficiency virus type 1 Vpr(34-51) peptide in micelle containing aqueous solution.
Eur.J.Biochem., 269:3264-3269, 2002
Cited by
PubMed Abstract: 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 alpha 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 alpha 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.
PubMed: 12084067
DOI: 10.1046/j.1432-1033.2002.03005.x
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

227111

数据于2024-11-06公开中

PDB statisticsPDBj update infoContact PDBjnumon