NDLI: Vipirinin, a Coumarin-based HIV-1 Vpr Inhibitor, Interacts with a Hydrophobic Region of VPR

Content Provider	Journal of Biological Chemistry (JBC)
Author	Ong, Eugene Boon Beng Watanabe, Nobumoto Saito, Akiko Futamura, Yushi Galil, Khaled Hussein Abd El Koito, Atsushi Najimudin, Nazalan Osada, Hiroyuki
Abstract	The human immunodeficiency virus 1 (HIV-1) viral protein R (Vpr) is an accessory protein that has been shown to have multiple roles in HIV-1 pathogenesis. By screening chemical libraries in the RIKEN Natural Products Depository, we identified a 3-phenyl coumarin-based compound that inhibited the cell cycle arrest activity of Vpr in yeast and Vpr-dependent viral infection of human macrophages. We determined its minimal pharmacophore through a structure-activity relationship study and produced more potent derivatives. We detected direct binding, and by assaying a panel of Vpr mutants, we found the hydrophobic region about residues Glu-25 and Gln-65 to be potentially involved in the binding of the inhibitor. Our findings exposed a targeting site on Vpr and delineated a convenient approach to explore other targeting sites on the protein using small molecule inhibitors as bioprobes.
Related Links	http://www.jbc.org/content/286/16/14049.abstract
Ending Page	14056
Starting Page	14049
Page Count	8
File Format	HTM / HTML PDF
ISSN	00219258
Journal	Journal of Biological Chemistry (JBC)
Issue Number	16
Volume Number	286
DOI	10.1074/jbc.M110.185397
e-ISSN	1083351X
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2011-04-22
Access Restriction	Open
Subject Keyword	AIDS Protein Drug Interactions Protein Structure Viral Protein Yeast Small Molecule Compounds Protein Structure and Folding
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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