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1biv
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(New page: 200px<br /><applet load="1biv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1biv" /> '''BOVINE IMMUNODEFICIENCY VIRUS TAT-TAR COMPLE...)
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Revision as of 09:34, 20 November 2007
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BOVINE IMMUNODEFICIENCY VIRUS TAT-TAR COMPLEX, NMR, 5 STRUCTURES
Overview
BACKGROUND: In lentiviruses such as human immunodeficiency virus (HIV) and, bovine immunodeficiency virus (BIV), the Tat (trans-activating) protein, enhances transcription of the viral RNA by complexing to the 5'-end of the, transcribed mRNA, at a region known as TAR (the trans-activation response, element). Identification of the determinants that account for specific, molecular recognition requires a high resolution structure of the Tat, peptide-TAR RNA complex. RESULTS: We report here on the structural, characterization of a complex of the recognition domains of BIV Tat and, TAR in aqueous solution using a combination of NMR and molecular dynamics., The 17-mer Tat peptide recognition domain folds into a beta-hairpin and, penetrates in an edge-on orientation deep into a widened major groove of, the 28-mer TAR RNA recognition domain in the complex. The RNA fold is, defined, in part, by two uracil bulged bases; U12 has a looped-out, conformation that widens the major groove and U10 forms a U.AU base triple, that buttresses the RNA helix. Together, these bulged bases induce a, approximately 40 degree bend between the two helical stems of the TAR RNA, in the complex. A set of specific intermolecular hydrogen bonds between, arginine side chains and the major-groove edge of guanine residues, contributes to sequence specificity. These peptide-RNA contacts are, complemented by other intermolecular hydrogen bonds and intermolecular, hydrophobic packing contacts involving glycine and isoleucine side chains., CONCLUSIONS: We have identified a new structural motif for protein-RNA, recognition, a beta-hairpin peptide that interacts with the RNA major, groove. Specificity is associated with formation of a novel RNA structural, motif, a U.AU base triple, which facilitates hydrogen bonding of an, arginine residue to a guanine and to a backbone phosphate. These results, should facilitate the design of inhibitors that can disrupt HIV Tat-TAR, association.
About this Structure
1BIV is a Single protein structure of sequence from Bovine immunodeficiency virus. Full crystallographic information is available from OCA.
Reference
Molecular recognition in the bovine immunodeficiency virus Tat peptide-TAR RNA complex., Ye X, Kumar RA, Patel DJ, Chem Biol. 1995 Dec;2(12):827-40. PMID:8807816
Page seeded by OCA on Tue Nov 20 11:41:12 2007
