PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 17690258-3 2007 We determined the crystal structure at 2.9 angstroms of the bacterial leucine transporter (LeuT), a homolog of SERT, NET, and DAT, in complex with leucine and the antidepressant desipramine. Leucine 70-77 solute carrier family 6 member 3 Homo sapiens 126-129 15953370-3 2005 To test this hypothesis, here we analysed transport activity for DAT mutants where this Pro was mutated into different amino acids, including Ser, Val, Leu and Phe. Leucine 152-155 solute carrier family 6 member 3 Homo sapiens 65-68 2078309-3 1990 The CSF concentrations of glycine, leucine and valine were also significantly reduced in the DAT cases. Leucine 35-42 solute carrier family 6 member 3 Homo sapiens 93-96 22192271-3 2011 FINDINGS: Here we present comparisons of the binding sites and the electrostatic potential surfaces (EPS) of DAT, NET and SERT homology models based on two different LeuTAa templates; with a substrate (leucine) in an occluded conformation (PDB id 2a65), and with an inhibitor (tryptophan) in an open-to-out conformation (PDB id 3f3a). Leucine 202-209 solute carrier family 6 member 3 Homo sapiens 109-112 34002696-6 2021 This is demonstrated by both Rosetta molecular modeling and fine-grained simulations using hDAT R445C, as well as EPR analysis and X-ray crystallography of the bacterial homolog leucine transporter. Leucine 178-185 solute carrier family 6 member 3 Homo sapiens 91-95