ArticleThe EMBO journal2025
Structural insights into binding-site access and ligand recognition by human ABCB1.
Article in The EMBO journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Cryo-EM structures of Cdr1 reveal snapshots of substrate transport and diverse inhibitor recognition.Science advances · 2026Article
- Breaking the Efflux Barrier: P-Glycoprotein and Emerging Strategies to Overcome Multidrug Resistance in Cancer.Cancers · 2026Review
- Review
- Functional implications of the conformational landscape of a multidrug transporter revealed by Zebrafish Abcb4 structures.Nature communications · 2026Article
- Characterizing P-glycoprotein and Breast Cancer Resistance Protein interactions of asciminib among other tyrosine kinase inhibitors used in chronic myeloid leukemia.Cancer chemotherapy and pharmacology · 2026Article
- A dual sensor regulates P-glycoprotein's structural plasticity.bioRxiv : the preprint server for biology · 2026Article
- Association ofFrontiers in cardiovascular medicine · 2026Article
- Integrated Modular Workflows for Membrane Protein Production in HEK293 Cells.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Understanding and overcoming multidrug resistance in cancer.Nature reviews. Clinical oncology · 2025Review
- P-glycoprotein modulates the fluidity gradient of the plasma membrane of multidrug resistant CHO cells.FEBS letters · 2025Article
- Cryo-EM Structures of Apo and DDT-Bound P-Glycoprotein in Yellowfin Tuna.Environmental science & technology · 2025Article
- P-Glycoprotein as a Therapeutic Target in Hematological Malignancies: A Challenge to Overcome.International journal of molecular sciences · 2025Review
- Mapping the Role of P-gp in Multidrug Resistance: Insights from Recent Structural Studies.International journal of molecular sciences · 2025Review
- Nucleotide asymmetry and flexible linker dynamics modulate drug efflux cycle of P-glycoprotein, A computational study.Computational and structural biotechnology journal · 2025Article
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5 authors.
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Abstract
ABCB1 is a broad-spectrum efflux pump central to cellular drug handling and multidrug resistance in humans. However, how it is able to recognize and transport a wide range of diverse substrates remains poorly understood. Here we present cryo-EM structures of lipid-embedded human ABCB1 in conformationally distinct apo-, substrate-bound, inhibitor-bound, and nucleotide-trapped states at 3.4-3.9 Å resolution, in the absence of stabilizing antibodies or mutations. The substrate-binding site is located within one half of the molecule and, in the apo state, is obstructed by the transmembrane helix (TM) 4. Substrate and inhibitor binding are distinguished by major TM rearrangements and their ligand binding chemistry, with TM4 playing a central role in all conformational transitions. Furthermore, our data identify secondary structure-breaking residues that impart localized TM flexibility and asymmetry between the two transmembrane domains. The resulting structural changes and lipid interactions that are induced by substrate and inhibitor binding can predict substrate-binding profiles and may direct ABCB1 inhibitor design.
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