ArticlePurinergic signalling2021
Substrate binding modes of purine and pyrimidine nucleotides to human ecto-5'-nucleotidase (CD73) and inhibition by their bisphosphonic acid derivatives.
Article in Purinergic signalling, 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, 18 citations in OpenAlex.
- Synthesis, biological evaluation and molecular docking studies of N-propylsulfonyl indole-linked hydrazinecarbothioamides as selective ecto-5'-nucleotidase and NTPDase inhibitors.Scientific reports · 2026Article
- Sym024 Interacts with a Unique Epitope on the CD73 Homodimer, Favoring Effective Bivalent Binding to Improve Anti-PD-1 Therapy.Clinical cancer research : an official journal of the American Association for Cancer Research · 2026Article
- Purinergic signaling modulates endothelial-to-mesenchymal transition in human aortic valve endothelial cells.BBA advances · 2026Article
- Advancing Intervertebral Disc Biology via Omics: Implications for Nucleus Pulposus Progenitor Cell-Based Regeneration.JOR spine · 2025Review
- CD39 and CD73: biological functions, diseases and therapy.Molecular biomedicine · 2025Review
- Synthesis, Characterization, Interactions, and Immunomodulatory Function of Ectonucleotidase CD39/CD73 Inhibitor 8-Butylthioadenosine 5'-Monophosphate.ACS pharmacology & translational science · 2025Article
- Article
- Roles of nucleotide metabolism in pancreatic cancer.Frontiers in immunology · 2025Review
- Cytokinins Reduce Viral Replication and Alter Plaque Morphology of Frog Virus 3 In Vitro.Viruses · 2024Article
- Structure-Activity Relationship of 3-Methylcytidine-5'-α,β-methylenediphosphates as CD73 Inhibitors.Journal of medicinal chemistry · 2022Article
- The Multifaceted Actions of CD73 During Development and Suppressive Actions of Regulatory T Cells.Frontiers in immunology · 2022Review
- Extracellular Nucleotides Affect the Proangiogenic Behavior of Fibroblasts, Keratinocytes, and Endothelial Cells.International journal of molecular sciences · 2021Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human ecto-5-nucleotidase (CD73) is involved in purinergic signalling, which influences a diverse range of biological processes. CD73 hydrolyses AMP and is the major control point for the levels of extracellular adenosine. Inhibitors of CD73 thus block the immunosuppressive action of adenosine, a promising approach for cancer immunotherapy. Interestingly, ADP and ATP are competitive inhibitors of CD73, with the most potent small-molecule inhibitors to date being non-hydrolysable ADP analogues. While AMP is the major substrate of the enzyme, CD73 has been reported to hydrolyse other 5'-nucleoside monophosphates. Based on a fragment screening campaign at the BESSY II synchrotron, we present the binding modes of various deoxyribo- and ribonucleoside monophosphates and of four additional fragments binding to the nucleoside binding site of the open form of the enzyme. Kinetic analysis of monophosphate hydrolysis shows that ribonucleotide substrates are favoured over their deoxyribose equivalents with AMP being the best substrate. We characterised the initial step of AMP hydrolysis, the binding mode of AMP to the open conformation of CD73 and compared that to other monophosphate substrates. In addition, the inhibitory activity of various bisphosphonic acid derivatives of nucleoside diphosphates was determined. Although AMPCP remains the most potent inhibitor, replacement of the adenine base with other purines or with pyrimidines increases the K
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