Cysteine Scanning Mutagenesis of Helices 2 and 7 in GLUT1 Identifies an Exofacial Cleft in Both Transmembrane Segments

Cysteine scanning mutagenesis in conjunction with site-directed chemical modification of sulfhydryl groups by p-chloromercuribenzenesulfonate (pCMBS) or N-ethylmaleimide (NEM) was applied to putative transmembrane segments (TM) 2 and 7 of the cysteine-less glucose transporter GLUT1. Valid for both h...

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Veröffentlicht in:	Biochemistry (Easton) 2000-03, Vol.39 (10), p.2469-2474
Hauptverfasser:	Olsowski, Andreas, Monden, Ingrid, Krause, Gerd, Keller, Konrad
Format:	Artikel
Sprache:	eng
Schlagworte:	4-Chloromercuribenzenesulfonate - metabolism Amino Acid Substitution - genetics Computer Simulation Cysteine - genetics Cysteine - metabolism Ethylmaleimide - metabolism Glucose Transporter Type 1 GLUT1 protein Glutamine - genetics Glutamine - metabolism Humans Isoleucine - genetics Isoleucine - metabolism Membrane Proteins - genetics Membrane Proteins - metabolism Models, Molecular Monosaccharide Transport Proteins - genetics Monosaccharide Transport Proteins - metabolism Mutagenesis, Site-Directed Protein Structure, Secondary Sulfhydryl Reagents - metabolism
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