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. 2021 Jun 15;16:278. doi: 10.1186/s13023-021-01902-5

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© The Author(s) 2021

Open AccessThis 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 4 — Evaluation of L277P mutation in CEP78. A Presentation of wildtype CEP78 protein 3D structure. B Mutant status of CEP78 protein. The amino acid at position 277 was mutated from leucine (LEU) to proline acid (PRO), leading to the loss of three hydrogen bonds between the wildtype LEU at residue 277 and Alanine acid (ALA) at residue 273, Lysine acid (LYS) at residue 274, and LEU at residue 280. C Alignment of CEP78 protein sequence from amino acid 267 to 287 to its orthologous protein sequences in different species indicated evolutionary conservation of leucine at position 277 in human CEP78. D Representations of relative linear locations of the L277P mutation in genome structure (top) and protein domains (bottom)