{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["11(12)"],"submitter":["Dai L"],"pubmed_abstract":["Heteromeric amino acid transporters (HATs), including y+LAT1-4F2hc complex, are responsible for transporting amino acids across membranes, and mutations in y+LAT1 cause lysinuric protein intolerance (LPI), a hereditary disorder characterized by defective cationic amino acid transport. The relationship between LPI and specific mutations in y+LAT1 has yet to be fully understood. In this study, we characterized the function of y+LAT1-4F2hc complex in mammalian cells and determined the cryo-EM structures of the human y+LAT1-4F2hc complex in two distinct conformations: the apo state in an inward-open conformation and the native substrate-bound state in an outward-open conformation. Structural analysis suggests that Asp243 in y+LAT1-4F2hc complex, are responsible for transporting amino acids across membranes, and mutations in y+LAT1 cause lysinuric protein intolerance (LPI), a hereditary disorder characterized by defective cationic amino acid transport. The relationship between LPI and specific mutations in y+LAT1 has yet to be fully understood. In this study, we characterized the function of y+LAT1-4F2hc complex in mammalian cells and determined the cryo-EM structures of the human y+LAT1-4F2hc complex in two distinct conformations: the apo state in an inward-open conformation and the native substrate-bound state in an outward-open conformation. Structural analysis suggests that Asp243 in y