1ull
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(New page: 200px<br /> <applet load="1ull" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ull" /> '''RNA APTAMER COMPLEXED WITH HIV-1 REV PEPTID...)
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Revision as of 12:27, 8 November 2007
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RNA APTAMER COMPLEXED WITH HIV-1 REV PEPTIDE, NMR, 7 STRUCTURES
Overview
A combined NMR-molecular dynamics approach has been applied to determine, the solution structure of a HIV-1 17-mer rev peptide bound to its 35-mer, high affinity RNA aptamer binding site. Complex formation involves, adaptive binding with the alpha-helical arginine-rich basic rev peptide, targeting a widened RNA major groove centred about adjacent G.A and, reversed A.A mismatches. We have also identified a U AU triple in the, aptamer complex with the Hoogsteen-paired uracil base sandwiched between, two arginine side chains. The intermolecular contacts identified in the, aptamer complex readily account for the consequences of peptide and RNA, mutations, as well as the results of previous in vitro selection, experiments. The details of molecular recognition associated with, targeting by rev of its high affinity RNA binding sites open new, opportunities for structure-based drug design strategies.
About this Structure
1ULL is a Single protein structure of sequence from Human immunodeficiency virus 1. Full crystallographic information is available from OCA.
Reference
Deep penetration of an alpha-helix into a widened RNA major groove in the HIV-1 rev peptide-RNA aptamer complex., Ye X, Gorin A, Ellington AD, Patel DJ, Nat Struct Biol. 1996 Dec;3(12):1026-33. PMID:8946856
Page seeded by OCA on Thu Nov 8 14:33:24 2007
Categories: Human immunodeficiency virus 1 | Single protein | Ellington, A.D. | Gorin, A. | Patel, D.J. | Ye, X. | Adaptive binding of peptide and rna in complex | Alpha-helix in widened rna major groove | Complex (rna aptamer/rev peptide) | Purine-purine mismatches | Rev peptide-rna recognition | Uau base triple
