Literature summary 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.
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
1.1.1.21 |
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
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
1.1.1.21 |
([5-(5-nitrofuran-2-yl)-1,3,4-oxadiazol-2-yl]sulfanyl)acetic acid |
crystallization data |
Homo sapiens |
|
1.1.1.21 |
2-(carboxymethyl)-1-oxo-1,2-dihydronaphtho[1,2-d]isothiazole-4-carboxylic acid 3,3-dioxide |
crystallization data |
Homo sapiens |
|
1.1.1.21 |
2-[2-(carboxymethoxy)-2-oxoethyl]-1-oxo-1,2-dihydronaphtho[1,2-d]isothiazole-4-carboxylic acid 3,3-dioxide |
crystallization data |
Homo sapiens |
|
1.1.1.21 |
Tolrestat |
- |
Homo sapiens |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.1.1.21 |
Homo sapiens |
P15121 |
isoform ALR2 |
- |