1kzs
From Proteopedia
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Structure of Human Immunodeficiency Virus Type 1 Vpr(34-51) Peptide in Aqueous TFE Solution
Overview
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.
About this Structure
1KZS is a Single protein structure of sequence from [1] with and as ligands. Full crystallographic information is available from OCA.
Reference
Structure of human immunodeficiency virus type 1 Vpr(34-51) peptide in micelle containing aqueous solution., Engler A, Stangler T, Willbold D, Eur J Biochem. 2002 Jul;269(13):3264-9. PMID:12084067
Page seeded by OCA on Fri Feb 15 16:15:53 2008
Categories: Single protein | Engler, A. | Stangler, T. | Willbold, D. | ACE | NH2 | Hiv-1 | Nmr | Peptide | Solution structure | Tfe | Vpr
