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

被引:0
作者
Farhat, Danny [1 ]
Rezaei, Fatemeh [1 ]
Lee, Jyh-Yeuan [1 ]
机构
[1] Univ Ottawa, Fac Med, Dept Biochem Microbiol & Immunol, Ottawa, ON, Canada
基金
加拿大健康研究院; 加拿大自然科学与工程研究理事会;
关键词
ABCG5; ABCG8; Cholesterol; Sitosterol; Stigmasterol; X-ray crystallography; Molecular docking;
D O I
10.1016/j.dib.2022.108754
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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 pro-tein functioning to remove ingested plant sterols provid-ing protection from their toxic effects, although, the struc-tural features behind substrate binding in ABCG5/G8 remain poorly resolved. Within this data article, we present ex-tended 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 im-ages 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).(c) 2022 The Author(s). Published by Elsevier Inc. This is an open access article under the CC BY license ( http://creativecommons.org/licenses/by/4.0/ )
引用
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页数:12
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