title: Structures of HIV TAR RNA-ligand complexes reveal higher binding stoichiometries.
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.
authors.affiliation: Institut für Organische Chemie und Chemische Biologie, Zentrum für Biomolekulare Magnetische Resonanz (BMRZ), Johann Wolfgang Goethe-Universität Frankfurt am Main, Max-von-Laue-Strasse 7, 60438 Frankfurt am Main, Germany.
authors.forename: Jan
authors.initials: J
authors.lastname: Ferner
authors.forename: Marcel
authors.initials: M
authors.lastname: Suhartono
authors.forename: Sven
authors.initials: S
authors.lastname: Breitung
authors.forename: Hendrik R A
authors.initials: HR
authors.lastname: Jonker
authors.forename: Mirko
authors.initials: M
authors.lastname: Hennig
authors.forename: Jens
authors.initials: J
authors.lastname: Wöhnert
authors.forename: Michael
authors.initials: M
authors.lastname: Göbel
authors.forename: Harald
authors.initials: H
authors.lastname: Schwalbe
mesh_terms: D001665:Binding Sites; D016325:HIV Long Terminal Repeat; D008024:Ligands; D009690:Nucleic Acid Conformation; D010455:Peptides / Q000737:chemistry; D012367:RNA, Viral / Q000737:chemistry*
chemical_list: D008024:Ligands; D010455:Peptides; D012367:RNA, Viral