1FI0
SOLUTION STRUCTURE OF HIV-1 VPR (13-33) PEPTIDE IN MICELLS
Summary for 1FI0
| Entry DOI | 10.2210/pdb1fi0/pdb |
| Descriptor | VPR PROTEIN (1 entity in total) |
| Functional Keywords | helix, viral protein |
| Total number of polymer chains | 1 |
| Total formula weight | 2614.88 |
| Authors | Engler, A.,Stangler, T.,Willbold, D. (deposition date: 2000-08-03, release date: 2001-02-28, Last modification date: 2024-10-30) |
| Primary citation | Engler, A.,Stangler, T.,Willbold, D. Solution structure of human immunodeficiency virus type 1 Vpr(13-33) peptide in micelles. Eur.J.Biochem., 268:389-395, 2001 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 G2 cell cycle arrest and is involved in cellular differentiation and cell death. Also, 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 obviously is dependent on its localization in or at membranes. We focused our structural studies on the secondary structure of a peptide consisting of residues 13-33 of HIV-1 Vpr in micelles. Employing nuclear magnetic resonance and circular dichroism spectroscopy we found this part of Vpr, known to be essential for nuclear localization, to be almost completely alpha helical. Our results provide structural data suggesting residues 13-33 of Vpr to form an amphipathic, leucine-zipper-like alpha helix that serves as a basis for interactions with a variety of viral and cellular factors. PubMed: 11168374DOI: 10.1046/j.1432-1033.2001.01895.x PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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