Data on structural analysis of cholesterol binding and sterol selectivity by ABCG5/G8
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Updated: Aug 16, 2025

Author Spotlight: A Bicelle Crystallization Setup for ABC Transporter Membrane Proteins to Advance Drug Development
Published on: August 25, 2023
Danny Farhat1, Fatemeh Rezaei1, Jyh-Yeuan Lee1
1Department of Biochemistry, Microbiology and Immunology, Faculty of Medicine, University of Ottawa, Ottawa, Ontario, Canada.
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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