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Data on structural analysis of cholesterol binding and sterol selectivity by ABCG5/G8

ATP-Binding cassette subfamily G (ABCG) sterol transporters maintain whole body endogenous and exogenous sterol homeostasis. A substantial portion of exogenous sterols are undigestible phytosterols (plant sterols), which can introduce complications when accumulated. ABCG5/G8 is the main protein func...

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Autores principales: Farhat, Danny, Rezaei, Fatemeh, Lee, Jyh-Yeuan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9747660/
https://www.ncbi.nlm.nih.gov/pubmed/36533288
http://dx.doi.org/10.1016/j.dib.2022.108754
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author Farhat, Danny
Rezaei, Fatemeh
Lee, Jyh-Yeuan
author_facet Farhat, Danny
Rezaei, Fatemeh
Lee, Jyh-Yeuan
author_sort Farhat, Danny
collection PubMed
description ATP-Binding cassette subfamily G (ABCG) sterol transporters maintain whole body endogenous and exogenous sterol homeostasis. A substantial portion of exogenous sterols are undigestible phytosterols (plant sterols), which can introduce complications when accumulated. ABCG5/G8 is the main protein functioning to remove ingested plant sterols providing protection from their toxic effects, although, the structural features behind substrate binding in ABCG5/G8 remain poorly resolved. Within this data article, we present extended preceding in the determination of the cholesterol-bound crystal structure and the sterol docking analysis. The crystal structure was deposited in the Protein Data Bank with the accession number of 8CUB, whereas the diffraction images were deposited at the SBGrid Data Bank. This dataset follows the research article entitled as “Structural analysis of cholesterol binding and sterol selectivity by ABCG5/G8” (doi: 10.1016/j.jmb.2022.167795).
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spelling pubmed-97476602022-12-15 Data on structural analysis of cholesterol binding and sterol selectivity by ABCG5/G8 Farhat, Danny Rezaei, Fatemeh Lee, Jyh-Yeuan Data Brief Data Article ATP-Binding cassette subfamily G (ABCG) sterol transporters maintain whole body endogenous and exogenous sterol homeostasis. A substantial portion of exogenous sterols are undigestible phytosterols (plant sterols), which can introduce complications when accumulated. ABCG5/G8 is the main protein functioning to remove ingested plant sterols providing protection from their toxic effects, although, the structural features behind substrate binding in ABCG5/G8 remain poorly resolved. Within this data article, we present extended preceding in the determination of the cholesterol-bound crystal structure and the sterol docking analysis. The crystal structure was deposited in the Protein Data Bank with the accession number of 8CUB, whereas the diffraction images were deposited at the SBGrid Data Bank. This dataset follows the research article entitled as “Structural analysis of cholesterol binding and sterol selectivity by ABCG5/G8” (doi: 10.1016/j.jmb.2022.167795). Elsevier 2022-11-17 /pmc/articles/PMC9747660/ /pubmed/36533288 http://dx.doi.org/10.1016/j.dib.2022.108754 Text en © 2022 The Author(s) https://creativecommons.org/licenses/by/4.0/This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Data Article
Farhat, Danny
Rezaei, Fatemeh
Lee, Jyh-Yeuan
Data on structural analysis of cholesterol binding and sterol selectivity by ABCG5/G8
title Data on structural analysis of cholesterol binding and sterol selectivity by ABCG5/G8
title_full Data on structural analysis of cholesterol binding and sterol selectivity by ABCG5/G8
title_fullStr Data on structural analysis of cholesterol binding and sterol selectivity by ABCG5/G8
title_full_unstemmed Data on structural analysis of cholesterol binding and sterol selectivity by ABCG5/G8
title_short Data on structural analysis of cholesterol binding and sterol selectivity by ABCG5/G8
title_sort data on structural analysis of cholesterol binding and sterol selectivity by abcg5/g8
topic Data Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9747660/
https://www.ncbi.nlm.nih.gov/pubmed/36533288
http://dx.doi.org/10.1016/j.dib.2022.108754
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