A possible recognition mode of mRNA cap terminal structure by peptide: cooperative stacking and hydrogen-bond pairing interactions between m7GpppA and Trp-Leu-Glu.
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.
Ueda
H
H
Osaka University of Pharmaceutical Sciences, Japan.
Doi
M
M
Inoue
M
M
Ishida
T
T
Tanaka
T
T
Uesugi
S
S
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
D002352:Carrier Proteins; D009842:Oligopeptides; D012314:RNA Cap Analogs; D039381:RNA Cap-Binding Proteins; D012315:RNA Caps; C056552:tryptophyl-leucyl-glutamic acid