Charged/Polar-Residue Scanning of the Hydrophobic Face of Transmembrane Domain 9 of the Yeast Glutathione Transporter, Hgt1p, Reveals a Conformationally Critical Region for Substrate Transport

Unraveling the mechanistic workings of membrane transporters has remained a challenging task. We describe a novel strategy that involves subjecting the residues of the hydrophobic face of a transmembrane helix to a charged/polar scanning mutagenesis. TMD9 of the yeast glutathione transporter, Hgt1p,...

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Detalles Bibliográficos
Autores principales: Thakur, Anil, Bachhawat, Anand K.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Genetics Society of America 2015
Materias:
Investigations
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4426376/
https://www.ncbi.nlm.nih.gov/pubmed/25784163
http://dx.doi.org/10.1534/g3.115.017079

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4426376/
https://www.ncbi.nlm.nih.gov/pubmed/25784163
http://dx.doi.org/10.1534/g3.115.017079

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