ArticleCommunications biology2023
Structural basis for substrate and inhibitor recognition of human multidrug transporter MRP4.
Article in Communications biology, 2023. 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.
- Inactivation of CDK12 Enhances Mitochondrial Efficiency to Suppress DNA Damage.Journal of cellular and molecular medicine · 2026Article
- Structural insights into toxicant export mediated by ABCC2 in Arabidopsis thaliana.Nature communications · 2025Article
- Protein Kinase A and assembly of an ABCC4 protein network.Nature communications · 2025Article
- Molecular basis of prostaglandin ENature communications · 2025Article
- Structural Basis for Oxidized Glutathione Recognition by Yeast Cadmium Factor 1.Journal of the American Chemical Society · 2025Article
- Structural basis of human ABCC4 recognition of cAMP and ligand recognition flexibility.Cell & bioscience · 2025Article
- Structures of ATP-binding cassette transporter ABCC1 reveal the molecular basis of cyclic dinucleotide cGAMP export.Immunity · 2025Article
- Differential Selectivity of Human and Mouse ABCC4/Abcc4 for Arsenic Metabolites.Drug metabolism and disposition: the biological fate of chemicals · 2024Article
- Inhibition and transport mechanisms of the ABC transporter hMRP5.Nature communications · 2024Article
- Structural View of Cryo-Electron Microscopy-Determined ATP-Binding Cassette Transporters in Human Multidrug Resistance.Biomolecules · 2024Review
- Comparing ATPase activity of ATP-binding cassette subfamily C member 4, lamprey CFTR, and human CFTR using an antimony-phosphomolybdate assay.Frontiers in pharmacology · 2024Article
- Estimating the true stability of the prehydrolytic outward-facing state in an ABC protein.eLife · 2023Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human multidrug resistance protein 4 (hMRP4, also known as ABCC4), with a representative topology of the MRP subfamily, translocates various substrates across the membrane and contributes to the development of multidrug resistance. However, the underlying transport mechanism of hMRP4 remains unclear due to a lack of high-resolution structures. Here, we use cryogenic electron microscopy (cryo-EM) to resolve its near-atomic structures in the apo inward-open and the ATP-bound outward-open states. We also capture the PGE1 substrate-bound structure and, importantly, the inhibitor-bound structure of hMRP4 in complex with sulindac, revealing that substrate and inhibitor compete for the same hydrophobic binding pocket although with different binding modes. Moreover, our cryo-EM structures, together with molecular dynamics simulations and biochemical assay, shed light on the structural basis of the substrate transport and inhibition mechanism, with implications for the development of hMRP4-targeted drugs.
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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.