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http://purl.uniprot.org/citations/32993041http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/32993041http://www.w3.org/2000/01/rdf-schema#comment"Heterodimeric amino acid transporters (HATs) are protein complexes mediating the transport of amino acids and derivatives thereof across biological membranes. HATs are composed of two subunits, a heavy and a light chain subunit belonging to the solute carrier (SLC) families SLC3 and SLC7. The human HAT 4F2hc-LAT2 is composed of the type-II membrane N-glycoprotein 4F2hc (SCL3A2) and the L-type amino acid transporter LAT2 (SLC7A8), which are covalently linked to each other by a conserved disulfide bridge. Whereas LAT2 catalyzes substrate transport, 4F2hc is important for the successful trafficking of the transporter to the plasma membrane. The overexpression, malfunction, or absence of 4F2hc-LAT2 is associated with human diseases, and therefore, this heterodimeric complex represents a potential drug target. The recombinant human 4F2hc-LAT2 can be functionally overexpressed in the methylotrophic yeast Pichia pastoris, and the protein can be purified. Here, we present the cryo-EM density map of the human 4F2hc-LAT2 amino acid transporter at sub-nanometer resolution. A homology model of 4F2hc-LAT2 in the inward-open conformation was generated and fitted into the cryo-EM density and analyzed. In addition, disease-causing point mutations in human LAT2 were mapped on the homology model of 4F2hc-LAT2, and the possible functional implications on the molecular level are discussed."xsd:string
http://purl.uniprot.org/citations/32993041http://purl.org/dc/terms/identifier"doi:10.3390/ijms21197094"xsd:string
http://purl.uniprot.org/citations/32993041http://purl.uniprot.org/core/author"Fotiadis D."xsd:string
http://purl.uniprot.org/citations/32993041http://purl.uniprot.org/core/author"Jeckelmann J.M."xsd:string
http://purl.uniprot.org/citations/32993041http://purl.uniprot.org/core/date"2020"xsd:gYear
http://purl.uniprot.org/citations/32993041http://purl.uniprot.org/core/name"Int J Mol Sci"xsd:string
http://purl.uniprot.org/citations/32993041http://purl.uniprot.org/core/pages"E7094"xsd:string
http://purl.uniprot.org/citations/32993041http://purl.uniprot.org/core/title"Sub-Nanometer Cryo-EM Density Map of the Human Heterodimeric Amino Acid Transporter 4F2hc-LAT2."xsd:string
http://purl.uniprot.org/citations/32993041http://purl.uniprot.org/core/volume"21"xsd:string
http://purl.uniprot.org/citations/32993041http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/32993041
http://purl.uniprot.org/citations/32993041http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/32993041
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http://purl.uniprot.org/uniprot/#_Q9UHI5-mappedCitation-32993041http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/32993041
http://purl.uniprot.org/uniprot/Q53EM9http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/32993041
http://purl.uniprot.org/uniprot/Q7Z4Z5http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/32993041
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