ArticleActa crystallographica. Section D, Biological crystallography2015
Three-dimensional structure of the human breast cancer resistance protein (BCRP/ABCG2) in an inward-facing conformation.
Article in Acta crystallographica. Section D, Biological crystallography, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
15 citing papers in PubMed, 36 citations in OpenAlex.
- Targeting breast cancer resistance protein (BCRP/ABCG2) in cancer.Translational cancer research · 2024Review
- Progress in Research of Nanotherapeutics for Overcoming Multidrug Resistance in Cancer.International journal of molecular sciences · 2024Review
- Acquired Drug Resistance Enhances Imidazoquinoline Efflux by P-Glycoprotein.Pharmaceuticals (Basel, Switzerland) · 2021Article
- Multidrug Resistance in Mammals and Fungi-From MDR to PDR: A Rocky Road from Atomic Structures to Transport Mechanisms.International journal of molecular sciences · 2021Review
- ABC transporter superfamily. An updated overview, relevance in cancer multidrug resistance and perspectives with personalized medicine.Molecular biology reports · 2021Review
- Review
- 3D structure of the transporter ABCG2-What's new?British journal of pharmacology · 2020Review
- Pharmacologic inducers of the uric acid exporter ABCG2 as potential drugs for treatment of gouty arthritis.Asian journal of pharmaceutical sciences · 2020Review
- Residues contributing to drug transport by ABCG2 are localised to multiple drug-binding pockets.The Biochemical journal · 2018Article
- Structure-function relationships in ABCG2: insights from molecular dynamics simulations and molecular docking studies.Scientific reports · 2017Article
- PharmGKB summary: very important pharmacogene information for ABCG2.Pharmacogenetics and genomics · 2017Review
- The structure of the human ABC transporter ABCG2 reveals a novel mechanism for drug extrusion.Scientific reports · 2017Article
- Structure of the human multidrug transporter ABCG2.Nature · 2017Article
- Enhancing Drug Efficacy and Therapeutic Index through Cheminformatics-Based Selection of Small Molecule Binary Weapons That Improve Transporter-Mediated Targeting: A Cytotoxicity System Based on Gemcitabine.Frontiers in pharmacology · 2017Article
- The multidrug transporter ABCG2: still more questions than answers.Biochemical Society transactions · 2016Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
ABCG2 is an efflux drug transporter that plays an important role in drug resistance and drug disposition. In this study, the first three-dimensional structure of human full-length ABCG2 analysed by electron crystallography from two-dimensional crystals in the absence of nucleotides and transported substrates is reported at 2 nm resolution. In this state, ABCG2 forms a symmetric homodimer with a noncrystallographic twofold axis perpendicular to the two-dimensional crystal plane, as confirmed by subtomogram averaging. This configuration suggests an inward-facing configuration similar to murine ABCB1, with the nucleotide-binding domains (NBDs) widely separated from each other. In the three-dimensional map, densities representing the long cytoplasmic extensions from the transmembrane domains that connect the NBDs are clearly visible. The structural data have allowed the atomic model of ABCG2 to be refined, in which the two arms of the V-shaped ABCG2 homodimeric complex are in a more closed and narrower conformation. The structural data and the refined model of ABCG2 are compatible with the biochemical analysis of the previously published mutagenesis studies, providing novel insight into the structure and function of the transporter.
Indexed as
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What OpenQuestion holds
Registered trials
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.