In silico characterization of the novel SDR42E1 as a potential vitamin D modulator

<p dir="ltr">The short-chain dehydrogenase/reductase (SDR) superfamily encompasses enzymes that play essential roles in the metabolism of steroid hormones and lipids. Despite an enigmatic function, recent genetic studies have linked the novel SDR 42 extended-1 (SDR42E1) gene to 25-hy...

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Main Author: Nagham Nafiz Hendi (17064261) (author)
Other Authors: Georges Nemer (295984) (author)
Published: 2024
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author Nagham Nafiz Hendi (17064261)
author2 Georges Nemer (295984)
author2_role author
author_facet Nagham Nafiz Hendi (17064261)
Georges Nemer (295984)
author_role author
dc.creator.none.fl_str_mv Nagham Nafiz Hendi (17064261)
Georges Nemer (295984)
dc.date.none.fl_str_mv 2024-01-08T06:00:00Z
dc.identifier.none.fl_str_mv 10.1016/j.jsbmb.2023.106447
dc.relation.none.fl_str_mv https://figshare.com/articles/journal_contribution/In_silico_characterization_of_the_novel_SDR42E1_as_a_potential_vitamin_D_modulator/26355064
dc.rights.none.fl_str_mv CC BY 4.0
info:eu-repo/semantics/openAccess
dc.subject.none.fl_str_mv Biological sciences
Biochemistry and cell biology
Bioinformatics and computational biology
SDR42E1
Vitamin D skin biosynthesis
Bioinformatics
Molecular docking
Evolutionary conservation
dc.title.none.fl_str_mv In silico characterization of the novel SDR42E1 as a potential vitamin D modulator
dc.type.none.fl_str_mv Text
Journal contribution
info:eu-repo/semantics/publishedVersion
text
contribution to journal
description <p dir="ltr">The short-chain dehydrogenase/reductase (SDR) superfamily encompasses enzymes that play essential roles in the metabolism of steroid hormones and lipids. Despite an enigmatic function, recent genetic studies have linked the novel SDR 42 extended-1 (SDR42E1) gene to 25-hydroxyvitamin D levels. This study investigated the potential <i>SDR42E1</i> functions and interactions with vitamin D using bioinformatics and molecular docking studies. Phylogenetic analysis unveiled that the nucleotide sequences of human SDR42E1 exhibit high evolutionary conservation across nematodes and fruit flies. Molecular docking analysis identified strong binding affinities between SDR42E1 and its orthologs with vitamin D3 and essential precursors, 8-dehydrocholesterol, followed by 7-dehydrocholesterol and 25-hydroxyvitamin D. The hydrophobic interactions observed between the protein residues and vitamin D compounds supported the predicted transmembrane localization of SDR42E1. Our investigation provides valuable insights into the potential role of SDR42E1 in skin vitamin D biosynthesis throughout species. This provides the foundation for future research and development of targeted therapies for vitamin D deficiency and related health conditions.</p><h2>Other Information</h2><p dir="ltr">Published in: The Journal of Steroid Biochemistry and Molecular Biology<br>License: <a href="https://creativecommons.org/licenses/by/4.0" target="_blank">https://creativecommons.org/licenses/by/4.0</a><br>See article on publisher's website: <a href="https://dx.doi.org/10.1016/j.jsbmb.2023.106447" target="_blank">https://dx.doi.org/10.1016/j.jsbmb.2023.106447</a></p>
eu_rights_str_mv openAccess
id Manara2_e82a2b0c103e62257caf9fc97710f426
identifier_str_mv 10.1016/j.jsbmb.2023.106447
network_acronym_str Manara2
network_name_str Manara2
oai_identifier_str oai:figshare.com:article/26355064
publishDate 2024
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rights_invalid_str_mv CC BY 4.0
spelling In silico characterization of the novel SDR42E1 as a potential vitamin D modulatorNagham Nafiz Hendi (17064261)Georges Nemer (295984)Biological sciencesBiochemistry and cell biologyBioinformatics and computational biologySDR42E1Vitamin D skin biosynthesisBioinformaticsMolecular dockingEvolutionary conservation<p dir="ltr">The short-chain dehydrogenase/reductase (SDR) superfamily encompasses enzymes that play essential roles in the metabolism of steroid hormones and lipids. Despite an enigmatic function, recent genetic studies have linked the novel SDR 42 extended-1 (SDR42E1) gene to 25-hydroxyvitamin D levels. This study investigated the potential <i>SDR42E1</i> functions and interactions with vitamin D using bioinformatics and molecular docking studies. Phylogenetic analysis unveiled that the nucleotide sequences of human SDR42E1 exhibit high evolutionary conservation across nematodes and fruit flies. Molecular docking analysis identified strong binding affinities between SDR42E1 and its orthologs with vitamin D3 and essential precursors, 8-dehydrocholesterol, followed by 7-dehydrocholesterol and 25-hydroxyvitamin D. The hydrophobic interactions observed between the protein residues and vitamin D compounds supported the predicted transmembrane localization of SDR42E1. Our investigation provides valuable insights into the potential role of SDR42E1 in skin vitamin D biosynthesis throughout species. This provides the foundation for future research and development of targeted therapies for vitamin D deficiency and related health conditions.</p><h2>Other Information</h2><p dir="ltr">Published in: The Journal of Steroid Biochemistry and Molecular Biology<br>License: <a href="https://creativecommons.org/licenses/by/4.0" target="_blank">https://creativecommons.org/licenses/by/4.0</a><br>See article on publisher's website: <a href="https://dx.doi.org/10.1016/j.jsbmb.2023.106447" target="_blank">https://dx.doi.org/10.1016/j.jsbmb.2023.106447</a></p>2024-01-08T06:00:00ZTextJournal contributioninfo:eu-repo/semantics/publishedVersiontextcontribution to journal10.1016/j.jsbmb.2023.106447https://figshare.com/articles/journal_contribution/In_silico_characterization_of_the_novel_SDR42E1_as_a_potential_vitamin_D_modulator/26355064CC BY 4.0info:eu-repo/semantics/openAccessoai:figshare.com:article/263550642024-01-08T06:00:00Z
spellingShingle In silico characterization of the novel SDR42E1 as a potential vitamin D modulator
Nagham Nafiz Hendi (17064261)
Biological sciences
Biochemistry and cell biology
Bioinformatics and computational biology
SDR42E1
Vitamin D skin biosynthesis
Bioinformatics
Molecular docking
Evolutionary conservation
status_str publishedVersion
title In silico characterization of the novel SDR42E1 as a potential vitamin D modulator
title_full In silico characterization of the novel SDR42E1 as a potential vitamin D modulator
title_fullStr In silico characterization of the novel SDR42E1 as a potential vitamin D modulator
title_full_unstemmed In silico characterization of the novel SDR42E1 as a potential vitamin D modulator
title_short In silico characterization of the novel SDR42E1 as a potential vitamin D modulator
title_sort In silico characterization of the novel SDR42E1 as a potential vitamin D modulator
topic Biological sciences
Biochemistry and cell biology
Bioinformatics and computational biology
SDR42E1
Vitamin D skin biosynthesis
Bioinformatics
Molecular docking
Evolutionary conservation