Phlorizin Recognition in a C-terminal Fragment of SGLT1 Studied by Tryptophan Scanning and Affinity Labeling

• Published in: The Journal of biological chemistry Vol. 278; no. 49; pp. 49154 - 49163
• Main Authors: Raja, M. Mobeen, Tyagi, Navneet K., Kinne, Rolf K.H.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 05.12.2003; American Society for Biochemistry and Molecular Biology
• Subjects: Affinity Labels; Amino Acid Sequence; Base Sequence; DNA Primers; Ligands; Membrane Glycoproteins - chemistry; Membrane Glycoproteins - genetics; Membrane Glycoproteins - metabolism; Molecular Sequence Data; Monosaccharide Transport Proteins - chemistry; Monosaccharide Transport Proteins - genetics; Monosaccharide Transport Proteins - metabolism; Mutagenesis, Site-Directed; Phlorhizin - metabolism; Protein Binding; Sodium-Glucose Transporter 1; Spectrometry, Fluorescence; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Structure-Activity Relationship; Tryptophan - chemistry

SGLT1 as a sodium/glucose cotransporter is strongly inhibited by phlorizin, a phloretin 2′-glucoside that has strong interactions with the C-terminal loop 13. We have examined phlorizin recognition by the protein by site-directed single Trp scanning mutagenesis experiments. Six mutants (Q581W, E591W...