
Identification of a gene, ABCG5, important in the regulation of dietary cholesterol absorption. Accumulation of dietary cholesterol in sitosterolemia caused by mutations in adjacent ABC transporters. The G5G8 structure provides a mechanistic framework for understanding sterol transport and the disruptive effects of mutations causing sitosterolaemia.īerge, K. The transmembrane domains are coupled to the nucleotide-binding sites by networks of interactions that differ between the active and inactive ATPases, reflecting the catalytic asymmetry of the transporter. The structure reveals a new transmembrane fold that is present in a large and functionally diverse superfamily of ABC transporters. Here we use crystallization in lipid bilayers to determine the X-ray structure of human G5G8 in a nucleotide-free state at 3.9 Å resolution, generating the first atomic model of an ABC sterol transporter. Mutations disrupting G5G8 cause sitosterolaemia, a disorder characterized by sterol accumulation and premature atherosclerosis.

The ABCG5/ABCG8 heterodimer (G5G8) mediates excretion of neutral sterols in liver and intestines 1, 2, 3, 4, 5. Journal of Solid State Chemistry 2018, 266, 112-120.ATP binding cassette (ABC) transporters play critical roles in maintaining sterol balance in higher eukaryotes.

Study of charge transfer interaction modes in the mixed Donor-Acceptor cocrystals of pyrene derivatives and TCNQ: A combined structural, thermal, spectroscopic, and hirshfeld surfaces analysis.


Daniel William Davies, Sang Kyu Park, Prapti Kafle, Hyunjoong Chung, Dafei Yuan, Joseph W.Understanding the Effects of Dielectric Property, Separation Distance, and Band Alignment on Interlayer Excitons in 2D Hybrid MoS2/WSe2 Heterostructures. This article is cited by 10 publications.
