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. 2022 Jan 17;23(2):986. doi: 10.3390/ijms23020986

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© 2022 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).

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Evolutionary sequence conservation and 3D structure of PYROXD2. (A) The multiple sequence alignment of PYROXD2 reveals the affected p.Gly426 residue is highly conserved. (B) The predicted 3D structure of wild-type PYROXD2 (AF-Q8N2H3-F1, AlphaFold, modelled in icn3d) highlighting the patient variant p.(Gly426Ser) is highlighted in yellow, and the wild-type residues affected by the frameshift variant p.(Val498Cysfs*79) are highlighted in red. (C) Structural regions (from icn3d) indicate that the frameshift variant starting at p.Val498 (region highlighted in yellow) affects a beta-fold region (amino acids 498–504) and two major alpha-helical regions (amino acids 506–513 and 565–578) of the PYROXD2 protein.