1AH4
PIG ALDOSE REDUCTASE, HOLO FORM
1AH4 の概要
| エントリーDOI | 10.2210/pdb1ah4/pdb |
| 分子名称 | ALDOSE REDUCTASE, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total) |
| 機能のキーワード | oxidoreductase, aldose reductase, inhibition, diabetes |
| 由来する生物種 | Sus scrofa (pig) |
| 細胞内の位置 | Cytoplasm: P80276 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 36567.44 |
| 構造登録者 | |
| 主引用文献 | 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 Cited by 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: 9195881DOI: 10.1016/S0969-2126(97)00216-5 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2 Å) |
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