ArticlePLoS biology2020
Cryo-EM structure of the human concentrative nucleoside transporter CNT3.
Article in PLoS biology, 2020. 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, 21 citations in OpenAlex.
- The SLC-ome of membrane transport: from molecular discovery to physiology and clinical applications.Physiological reviews · 2026Review
- Extracellular Vesicle-Mediated Regulation of H3C14 Contributes to Gemcitabine Resistance in Bladder Cancer.Journal of extracellular vesicles · 2025Article
- Antiviral drug recognition and elevator-type transport motions of CNT3.Nature chemical biology · 2024Article
- Oligomerization of drug transporters: Forms, functions, and mechanisms.Acta pharmaceutica Sinica. B · 2024Review
- Identification of core therapeutic targets for Monkeypox virus and repurposing potential of drugs: A WEB prediction approach.PloS one · 2024Article
- Targeting SLC transporters: small molecules as modulators and therapeutic opportunities.Trends in biochemical sciences · 2023Review
- Structural basis of the substrate recognition and inhibition mechanism of Plasmodium falciparum nucleoside transporter PfENT1.Nature communications · 2023Article
- Inborn Errors of Nucleoside Transporter (NT)-Encoding Genes (International journal of molecular sciences · 2022Review
- A Historical Review of Brain Drug Delivery.Pharmaceutics · 2022Review
- Peptide Tags and Domains for Expression and Detection of Mammalian Membrane Proteins at the Cell Surface.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Molecular mechanism underlying transport and allosteric inhibition of bicarbonate transporter SbtA.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Toward a Molecular Basis of Cellular Nucleoside Transport in Humans.Chemical reviews · 2021Review
- Review
- Molecular basis for substrate recognition by the bacterial nucleoside transporter NupG.The Journal of biological chemistryArticle
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Concentrative nucleoside transporters (CNTs), members of the solute carrier (SLC) 28 transporter family, facilitate the salvage of nucleosides and therapeutic nucleoside derivatives across the plasma membrane. Despite decades of investigation, the structures of human CNTs remain unknown. We determined the cryogenic electron microscopy (cryo-EM) structure of human CNT (hCNT) 3 at an overall resolution of 3.6 Å. As with its bacterial homologs, hCNT3 presents a trimeric architecture with additional N-terminal transmembrane helices to stabilize the conserved central domains. The conserved binding sites for the substrate and sodium ions unravel the selective nucleoside transport and distinct coupling mechanism. Structural comparison of hCNT3 with bacterial homologs indicates that hCNT3 is stabilized in an inward-facing conformation. This study provides the molecular determinants for the transport mechanism of hCNTs and potentially facilitates the design of nucleoside 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.