Membrane topological structure of neutral system N/A amino acid transporter 4 (SNAT4) protein.

ABSTRACT: Members of system N/A amino acid transporter (SNAT) family mediate transport of neutral amino acids, including l-alanine, l-glutamine, and l-histidine, across the plasma membrane and are involved in a variety of cellular functions. By using chemical labeling, glycosylation, immunofluorescence combined with molecular modeling approaches, we resolved the membrane topological structure of SNAT4, a transporter expressed predominantly in liver. To analyze the orientation using the chemical labeling and biotinylation approach, the "Cys-null" mutant of SNAT4 was first generated by mutating all five endogenous cysteine residues. Based on predicted topological structures, a single cysteine residue was introduced individually into all possible nontransmembrane domains of the Cys-null mutant. The cel

SUBMITTER: Shi Q 

PROVIDER: S-EPMC3207422 | biostudies-literature | 2011 Nov

REPOSITORIES: biostudies-literature