title: A possible recognition mode of mRNA cap terminal structure by peptide: cooperative stacking and hydrogen-bond pairing interactions between m7GpppA and Trp-Leu-Glu.
abstract: 1H-NMR and fluorescence spectroscopic studies on the interaction between the Trp-Leu-Glu and m7GpppA have shown a specific binding mode, in which the pi-pi stacking interaction of the Trp indole ring and the hydrogen-bond pairing of Glu carboxyl side group with 7-methylguanine base are simultaneously formed.
authors.affiliation: Osaka University of Pharmaceutical Sciences, Japan.
authors.forename: H
authors.initials: H
authors.lastname: Ueda
authors.forename: M
authors.initials: M
authors.lastname: Doi
authors.forename: M
authors.initials: M
authors.lastname: Inoue
authors.forename: T
authors.initials: T
authors.lastname: Ishida
authors.forename: T
authors.initials: T
authors.lastname: Tanaka
authors.forename: S
authors.initials: S
authors.lastname: Uesugi
mesh_terms: D001482:Base Composition; D002352:Carrier Proteins; D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D009842:Oligopeptides; D011487:Protein Conformation; D012314:RNA Cap Analogs; D039381:RNA Cap-Binding Proteins; D012315:RNA Caps / Q000235:genetics*; D013050:Spectrometry, Fluorescence
chemical_list: D002352:Carrier Proteins; D009842:Oligopeptides; D012314:RNA Cap Analogs; D039381:RNA Cap-Binding Proteins; D012315:RNA Caps; C056552:tryptophyl-leucyl-glutamic acid