2ALR

ALDEHYDE REDUCTASE

「1ALR」から置き換えられました

2ALR の概要

• エントリーDOI: 10.2210/pdb2alr/pdb
• 分子名称: ALDEHYDE REDUCTASE (1 entity in total)
• 機能のキーワード: oxidoreductase, tim-barrel
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36486.77

構造登録者

El-Kabbani, O. (登録日: 1994-09-06, 公開日: 1996-06-20, 最終更新日: 2024-02-14)

主引用文献

El-Kabbani, O.,Green, N.C.,Lin, G.,Carson, M.,Narayana, S.V.,Moore, K.M.,Flynn, T.G.,DeLucas, L.J.
Structures of human and porcine aldehyde reductase: an enzyme implicated in diabetic complications.
Acta Crystallogr.,Sect.D, 50:859-868, 1994

PubMed Abstract: The crystal structures of porcine and human aldehyde reductase, an enzyme implicated in complications of diabetes, have been determined by X-ray diffraction methods. The crystallographic R factor for the refined porcine aldehyde reductase model is 0.19 at 2.8 A resolution. There are two molecules in the asymmetric unit related by a local non-crystallographic twofold axis. The human aldehyde reductase model has been refined to an R factor of 0.21 at 2.48 A resolution. The amino-acid sequence of porcine aldehyde reductase revealed a remarkable homology with human aldehyde reductase. The coenzyme-binding site residues are conserved and adopt similar conformations in human and porcine aldehyde reductase apo-enzymes. The tertiary structures of aldhyde reductase and aldose reductase are similar and consist of a beta/alpha-barrel, with the coenzyme-binding site located at the carboxy-terminus end of the strands of the barrel. The crystal structure of porcine and human aldehyde reductase should allow in vitro mutagenesis to elucidate the mechanism of action for this enzyme and facilitate the effective design of specific inhibitors.

PubMed: 15299353
DOI: 10.1107/S0907444994005275

実験手法

X-RAY DIFFRACTION (2.48 Å)