Ecto-5’-nucleotidase (e5NT) hydrolyzes extracellular nucleotides and contributes to purinergic
signaling. e5NT is implicated in a variety of pathological states including immunological diseases and cancer
and represents an emerging drug target. Herein, we review structural and computational studies that have
helped to better understand ligand binding characteristics and mechanistic features of the enzyme and led to
the identification of new classes of e5NT inhibitors.
Keywords: Catalytic mechanism, computational design, Ecto-5’-nucleotidase, inhibitors, virtual screening, x-ray crystallography.
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