ArticleData in brief2022
Data on structural analysis of cholesterol binding and sterol selectivity by ABCG5/G8.
Article in Data in brief, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
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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