ArticleCommunications biology2021
Cryo-EM structure of ABCG5/G8 in complex with modulating antibodies.
Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
- FKBP8 connects the Hsp70-Hsp90 chaperone machinery to the folding of membrane proteins.Nature communications · 2026Article
- Lipid transport mechanisms in human ABCA family transporters: a structural perspective.Biochemical Society transactions · 2026Review
- Visual exoproteomics ofbioRxiv : the preprint server for biology · 2026Article
- Revisiting the Role of the Leucine Plug/Valve in the Human ABCG2 Multidrug Transporter.International journal of molecular sciences · 2025Article
- Polydatin prevents cholesterol gallstone formation by regulating cholesterol metabolism via PPAR-γ signaling.Open life sciences · 2025Article
- ATP-Binding Cassette and Solute Carrier Transporters: Understanding Their Mechanisms and Drug Modulation Through Structural and Modeling Approaches.Pharmaceuticals (Basel, Switzerland) · 2024Review
- Structural basis for abscisic acid efflux mediated by ABCG25 in Arabidopsis thaliana.Nature plants · 2023Article
- Snapshots of ABCG1 and ABCG5/G8: A Sterol's Journey to Cross the Cellular Membranes.International journal of molecular sciences · 2022Review
- Data on structural analysis of cholesterol binding and sterol selectivity by ABCG5/G8.Data in brief · 2022Article
- Membranes under the Magnetic Lens: A Dive into the Diverse World of Membrane Protein Structures Using Cryo-EM.Chemical reviews · 2022Review
- Ins and outs of AlphaFold2 transmembrane protein structure predictions.Cellular and molecular life sciences : CMLS · 2022Article
- Binding mode analysis of ABCA7 for the prediction of novel Alzheimer's disease therapeutics.Computational and structural biotechnology journal · 2021Article
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The heterodimer of ATP-binding cassette transporter ABCG5 and ABCG8 mediates the excretion of sterols from liver and intestine, playing a critical role in cholesterol homeostasis. Here, we present the cryo-EM structure of ABCG5/G8 in complex with the Fab fragments from two monoclonal antibodies at 3.3Å resolution. The high-resolution structure reveals a unique dimer interface between the nucleotide-binding domains (NBD) of opposing transporters, consisting of an ordered network of salt bridges between the conserved NPXDFXXD motif and serving as a pivot point that may be important for the transport cycle. While mAb 11F4 increases the ATPase activity potentially by stabilization of the NBD dimer formation, mAb 2E10 inhibits ATP hydrolysis, likely by restricting the relative movement between the RecA and helical domain of ABCG8 NBD. Our study not only provides insights into the structural elements important for the transport cycle but also reveals novel epitopes for potential therapeutic interventions.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.