1AH0

PIG ALDOSE REDUCTASE COMPLEXED WITH SORBINIL

Summary for 1AH0

• Entry DOI: 10.2210/pdb1ah0/pdb
• Descriptor: ALDOSE REDUCTASE, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, SORBINIL, ... (4 entities in total)
• Functional Keywords: oxidoreductase, sorbinil inhibitor, diabetes
• Biological source: Sus scrofa (pig)
• Cellular location: Cytoplasm: P80276
• Total number of polymer chains: 1
• Total formula weight: 36787.64

Authors

Moras, D.,Podjarny, A.D. (deposition date: 1997-04-11, release date: 1998-04-15, Last modification date: 2024-04-03)

Primary citation

Urzhumtsev, A.,Tete-Favier, F.,Mitschler, A.,Barbanton, J.,Barth, P.,Urzhumtseva, L.,Biellmann, J.F.,Podjarny, A.,Moras, D.
A 'specificity' pocket inferred from the crystal structures of the complexes of aldose reductase with the pharmaceutically important inhibitors tolrestat and sorbinil.
Structure, 5:601-612, 1997

PubMed Abstract: Aldose reductase (AR) is an NADPH-dependent enzyme implicated in long-term diabetic complications. Buried at the bottom of a deep hydrophobic cleft, the NADPH coenzyme is surrounded by the conserved hydrophilic residues of the AR active site. The existence of an anionic binding site near the NADP+ has been determined from the structures of the complexes of AR with citrate, cacodylate and glucose-6-phosphate. The inhibitor zopolrestat binds to this anionic site, and in the hydrophobic cleft, after a change of conformation which opens a 'specificity' pocket.

PubMed: 9195881
DOI: 10.1016/S0969-2126(97)00216-5

Experimental method

X-RAY DIFFRACTION (2.3 Å)