1fi0 | pdb_00001fi0

SOLUTION STRUCTURE OF HIV-1 VPR (13-33) PEPTIDE IN MICELLS

spinqualitylabelsall models 1fi0, 22 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1fi0 is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: ACE Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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. Solution structure of human immunodeficiency virus type 1 Vpr(13-33) peptide in micelles.,Engler A, Stangler T, Willbold D Eur J Biochem. 2001 Jan;268(2):389-95. PMID:11168374 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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