1EL3

HUMAN ALDOSE REDUCTASE COMPLEXED WITH IDD384 INHIBITOR

1EL3 の概要

• エントリーDOI: 10.2210/pdb1el3/pdb
• 分子名称: ALDOSE REDUCTASE, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, [2,6-DIMETHYL-4-(2-O-TOLYL-ACETYLAMINO)-BENZENESULFONYL]-GLYCINE, ... (4 entities in total)
• 機能のキーワード: aldose reductase, inhibition, diabetes, oxidoreductase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: P15121
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37032.20

構造登録者

Podjarny, A. (登録日: 2000-03-13, 公開日: 2000-05-10, 最終更新日: 2024-04-03)

主引用文献

Calderone, V.,Chevrier, B.,Van Zandt, M.,Lamour, V.,Howard, E.,Poterszman, A.,Barth, P.,Mitschler, A.,Lu, J.,Dvornik, D.M.,Klebe, G.,Kraemer, O.,Moorman, A.R.,Moras, D.,Podjarny, A.
The structure of human aldose reductase bound to the inhibitor IDD384.
Acta Crystallogr.,Sect.D, 56:536-540, 2000

PubMed Abstract: The crystallographic structure of the complex between human aldose reductase (AR2) and one of its inhibitors, IDD384, has been solved at 1.7 A resolution from crystals obtained at pH 5.0. This structure shows that the binding of the inhibitor's hydrophilic head to the catalytic residues Tyr48 and His110 differs from that found previously with porcine AR2. The difference is attributed to a change in the protonation state of the inhibitor (pK(a) = 4.52) when soaked with crystals of human (at pH 5.0) or pig lens AR2 (at pH 6.2). This work demonstrates how strongly the detailed binding of the inhibitor's polar head depends on its protonation state.

PubMed: 10771421
DOI: 10.1107/S0907444900002341

実験手法

X-RAY DIFFRACTION (1.7 Å)