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. 2023 Nov 16;14:1283907. doi: 10.3389/fendo.2023.1283907

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Copyright © 2023 Lee, Tsai, Chang, Chen, Fann, Chang, Liu, Wu, Chiu, Hsu, Yang, Lai, Tsai, Yang and Chen

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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Structural prediction of SUR1 L366 and its interacting partner L1288 of K_ATP channel. In wild-type K_ATP channel, SUR1 L366 (red) could contact freely with its partner L1288 (red) via hydrophobic interaction in both Apo (PDB: 6JB1) and MgATP + MgADP bound form (PDB:6C3P) (upper panel). In contrast, in the hSUR1-L366F mutant K_ATP channel, the bulky phenylalanine (yellow) produces steric clashes against L1288 and consequently prevents the MgADP-induced conformational changes of SUR1 (lower panel).