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Structures of HIV TAR RNA–Ligand Complexes Reveal Higher Binding Stoichiometries
Authors:Jan Ferner  Marcel Suhartono Dr.  Sven Breitung  Hendrik R. A. Jonker Dr.  Mirko Hennig Prof. Dr.  Jens Wöhnert Prof. Dr.  Michael Göbel Prof. Dr.  Harald Schwalbe Prof. Dr.
Affiliation:1. Institut für Organische Chemie und Chemische Biologie, Zentrum für Biomolekulare Magnetische Resonanz (BMRZ), Johann Wolfgang Goethe‐Universit?t Frankfurt am Main, Max‐von‐Laue‐Strasse 7, 60438 Frankfurt am Main (Germany), Fax: (+49)?69‐798‐29515;2. Institut für Organische Chemie und Chemische Biologie, Johann Wolfgang Goethe‐Universit?t Frankfurt am Main, Max‐von‐Laue‐Strasse 7, 60438 Frankfurt am Main (Germany);3. Department of Biochemistry and Molecular Biology, Medical University of South Carolina, 173 Ashley Avenue, PO Box 250509, Charleston, SC 29425 (USA);4. Institut für Molekulare Biowissenschaften, Zentrum für Biomolekulare Magnetische Resonanz (BMRZ), Johann Wolfgang Goethe‐Universit?t Frankfurt am Main, Max‐von‐Laue‐Strasse 9, 60438 Frankfurt am Main (Germany)
Abstract:Target TAR by NMR : Tripeptides containing arginines as terminal residues and non‐natural amino acids as central residues are good leads for drug design to target the HIV trans‐activation response element (TAR). The structural characterization of the RNA–ligand complex by NMR spectroscopy reveals two specific binding sites that are located at bulge residue U23 and around the pyrimidine‐stretch U40‐C41‐U42 directly adjacent to the bulge.
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Keywords:HIV TAR ligands  NMR spectroscopy  peptides  RNA structures  RNA
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