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Literature summary for 3.1.3.5 extracted from

  • Knapp, K.; Zebisch, M.; Pippel, J.; El-Tayeb, A.; Mueller, C.E.; Straeter, N.
    Crystal structure of the human ecto-5-nucleotidase (CD73): insights into the regulation of purinergic signaling (2012), Structure, 20, 2161-2173.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with adenosine, inhibitors 2,2'-(2-(2-((2S,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-carboxamido)ethylamino)-2-oxoethylazanediyl) diacetic acid, baicalin and ADP analog AMPCP. The dimeric enzyme undergoes an extensive 114° conformational switch between the open and closed forms. The dimerization interface is formed by the C-terminal domains and exhibits interchain motions of up to 13°. Structural control of the domain movement determines the selectivity for monophosphate nucleotides Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
2,2'-(2-(2-((2S,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-carboxamido)ethylamino)-2-oxoethylazanediyl) diacetic acid nucleotide-derived inhibitor Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P21589
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Synonyms

Synonyms Comment Organism
NT5E
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Homo sapiens