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. 2022 Sep 6;10:920741. doi: 10.3389/fped.2022.920741

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Copyright © 2022 Yang, Liu, Chen, Lin, Wang, Chen, Wang and Yan.

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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(A) PyMOL software analysis: Ser869 interacts with Asp868 via hydrogen bonding in wild-type p.Ser869 in SETBP1; (B) PyMOL software analysis: no hydrogen-bond interaction between Gly869 and Asp868 in mutant-type p.Ser869 in SETBP1, indicating that variants affect protein structure and function; (C) Alignment of the SETBP1 sequences revealed that the amino acid residues at position 869 were strictly conserved.