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• W2965762486 endingPage "1900075" @default.
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• W2965762486 abstract "Ecto-5′-nucleotidase (CD73, EC 3.1.3.5) catalyzes the extracellular hydrolysis of AMP yielding adenosine, which induces immunosuppression, angiogenesis, metastasis, and proliferation of cancer cells. CD73 inhibition is therefore proposed as a novel strategy for cancer (immuno)therapy, and CD73 antibodies are currently undergoing clinical trials. Despite considerable efforts, the development of small molecule CD73 inhibitors has met with limited success. To develop a suitable drug candidate, a high resolution (2.05 Å) co-crystal structure of the CD73 inhibitor PSB-12379, a nucleotide analogue, in complex with human CD73 is determined. This allows the rational design and development of a novel inhibitor (PSB-12489) with subnanomolar inhibitory potency toward human and rat CD73, high selectivity, as well as high metabolic stability. A co-crystal structure of PSB-12489 with CD73 (1.85 Å) reveals the interactions responsible for increased potency. PSB-12489 is the most potent CD73 inhibitor to date representing a powerful tool compound and novel lead structure." @default.
• W2965762486 created "2019-08-13" @default.
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• W2965762486 date "2019-07-31" @default.
• W2965762486 modified "2023-10-15" @default.
• W2965762486 title "X‐Ray Co‐Crystal Structure Guides the Way to Subnanomolar Competitive Ecto‐5′‐Nucleotidase (CD73) Inhibitors for Cancer Immunotherapy" @default.
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• W2965762486 doi "https://doi.org/10.1002/adtp.201900075" @default.
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