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Literature summary for 1.1.1.21 extracted from

  • Steuber, H.; Zentgraf, M.; La Motta, C.; Sartini, S.; Heine, A.; Klebe, G.
    Evidence for a novel binding site conformer of aldose reductase in ligand-bound state (2007), J. Mol. Biol., 369, 186-197.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with inhibitors tolrestat, 2-(carboxymethyl)-1-oxo-1,2-dihydronaphtho[1,2-d]isothiazole-4-carboxylic acid 3,3-dioxide and 2-[2-(carboxymethoxy)-2-oxoethyl]-1-oxo-1,2-dihydronaphtho[1,2-d]isothiazole-4-carboxylic acid 3,3-dioxide. Unlike tolrestat, the naphthol[1,2-d]isothiazole inhibitors leave the specificity pocket in the closed state and ligand 2-(carboxymethyl)-1-oxo-1,2-dihydronaphtho[1,2-d]isothiazole-4-carboxylic acid 3,3-dioxide extends the catalytic pocket by opening a novel subpocket. Inhibitor 2-[2-(carboxymethoxy)-2-oxoethyl]-1-oxo-1,2-dihydronaphtho[1,2-d]isothiazole-4-carboxylic acid 3,3-dioxide provokes less pronounced induced-fit adaptations of the binding cavity Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
([5-(5-nitrofuran-2-yl)-1,3,4-oxadiazol-2-yl]sulfanyl)acetic acid crystallization data Homo sapiens
2-(carboxymethyl)-1-oxo-1,2-dihydronaphtho[1,2-d]isothiazole-4-carboxylic acid 3,3-dioxide crystallization data Homo sapiens
2-[2-(carboxymethoxy)-2-oxoethyl]-1-oxo-1,2-dihydronaphtho[1,2-d]isothiazole-4-carboxylic acid 3,3-dioxide crystallization data Homo sapiens
Tolrestat
-
Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P15121 isoform ALR2
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