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. 2020 Nov 10;6:82. doi: 10.1038/s41421-020-00207-4

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© The Author(s) 2020

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 1 — a The overall Cryo-EM map of the human LAT2–4F2hc + Leu complex. LAT2 and 4F2hc are cyan and wheat, respectively. b Overall structure of the LAT2–4F2hc + Leu complex. The glycosylation moieties are shown as sticks. H helix, TM transmembrane domain, ECD extracellular domain. c The Leu-binding site. d The Trp-binding site. Trp substrate might have two binding positions. e Mutations of the Trp-binding residues lead to a decreased transport activity. Data are mean ± s.d. of three independent experiments. f The two separated pockets in LAT2. The pockets 1 and 2 are separated by the substrate. g The water distribution in the pocket 2 of LAT2. h The alignment of the second pocket of LAT1 with LAT2. The residues of LAT1 and LAT2 are shown as yellow and cyan, respectively.