1rpv
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(New page: 200px<br /> <applet load="1rpv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rpv" /> '''HIV-1 REV PROTEIN (RESIDUES 34-50)'''<br />...)
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Revision as of 12:19, 8 November 2007
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HIV-1 REV PROTEIN (RESIDUES 34-50)
Overview
NMR spectroscopy has been used to solve the three-dimensional solution, structure of a minimal RNA-binding domain of the Rev protein from the, human immunodeficiency virus (type 1), an essential regulatory protein for, viral replication. The presence of 10 arginine residues in the 17-residue, peptide Rev34-50 caused significant problems in assignment of the NMR, spectra. To improve spectral resolution, the peptide was synthesized with, an alanine replacing a nonessential arginine and with selectively, 15N-labeled residues. Contrary to Chou-Fasman modeling predictions an, alpha-helix was detected in both water and 20% trifluoroethanol (TFE) and, was found to span residues that constitute the RNA-binding and, nuclear-localizing domains of Rev. The sequence-specific information, provided by the NMR data gives a full description of the solution, conformation of Rev34-50 which serves as a template for investigating, binding of the peptide to RNA from the Rev response element (RRE)., Preliminary modeling suggests that the helix can fit neatly into the, expanded major groove of the RRE where interactions between the peptide, side chains and the RNA can be identified. These data may aid the, construction of a suitable pharmacophore model for the rational design of, molecules that block Rev-RNA binding and inhibit HIV replication.
About this Structure
1RPV is a Single protein structure of sequence from Human immunodeficiency virus type 1 (isolate 12) with NH2 as ligand. Full crystallographic information is available from OCA.
Reference
NMR solution structure of the RNA-binding peptide from human immunodeficiency virus (type 1) Rev., Scanlon MJ, Fairlie DP, Craik DJ, Englebretsen DR, West ML, Biochemistry. 1995 Jul 4;34(26):8242-9. PMID:7599117
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