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. 2022 Sep 2;12:988290. doi: 10.3389/fonc.2022.988290

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Copyright © 2022 Nong, Zhang, Wang, Ding, Ji and Wu

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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The molecular structures of different types of BCAT protein sequences. Panel (A) shows the folded structures of human, rat and mouse BCAT 1 respectively, and their ligand maps, all of which depend on and bind to the cofactor PLP, and the binding ligands are all 4-METHYL VALERIC ACID (4MV). Panel (B) shows the folded structures of human, rat, and mouse BCAT2, respectively. Among them, the ligand that binds to human and mouse BCAT2 is 3-({(3R)-1-[(5-bromothiophen-2-yl)carbonyl]pyrrolidin-3-yl}oxy) -N-methyl-2’-[(methylsulfonyl)amino]biphenyl-4-carboxamide (EL1), and the ligand is shown in the figure. The ligand that binds to rat BCAT2 is 2-hydroxy-N-[(1R)-1,2,3,4-tetrahydronaphthalen-1-yl]acetamide (67Y), and the ligand is shown in the figure. All the structural diagrams are drawn on the mapping software SWISS-MODEL. The protein sequence of BCAT is input on the software to export the structural diagram.