AustralieFrV1, Main, Exploration, bibRecord, 00A425

Structure of aldehyde reductase holoenzyme in complex with the potent aldose reductase inhibitor fidarestat : Implications for inhibitor binding and selectivity

Identifieur interne : 00A425 ( Main/Exploration ); précédent : 00A424; suivant : 00A426

Structure of aldehyde reductase holoenzyme in complex with the potent aldose reductase inhibitor fidarestat : Implications for inhibitor binding and selectivity

Auteurs : Ossama El-Kabbani [Australie] ; Vincenzo Carbone [Australie] ; Connie Darmanin [Australie] ; Mitsuru Oka [Japon] ; Andre Mitschler [France] ; Alberto Podjarny [France] ; Clemens Schulze-Briese [Suisse] ; Roland P.-T. Chung [Australie]

Source :

Journal of medicinal chemistry : (Print) [ 0022-2623 ] ; 2005.

RBID : Pascal:06-0032107

Descripteurs français

Pascal (Inist)
- Aldehyde reductase, Inhibiteur enzyme, Fidarestat, Sélectivité, Complexe enzyme inhibiteur, Site actif, Liaison hydrogène, Structure cristalline, Modèle moléculaire, Porc, Isozyme, Diffraction RX, Structure moléculaire, Modélisation, Animal, Inhibiteur aldose reductase, Spiro[1-benzopyrane-4:4′-imidazole-2-carboxamide] dérivé.

English descriptors

KwdEn :
- Active site, Aldehyde reductase, Animal, Crystalline structure, Enzyme inhibitor, Fidarestat, Hydrogen bond, Inhibitor enzyme complex, Isozyme, Modeling, Molecular model, Molecular structure, Pig, Selectivity, X ray diffraction.

Abstract

Structure determination of porcine aldehyde reductase holoenzyme in complex with the potent aldose reductase inhibitor fidarestat was carried out to explain the difference in the potency of the inhibitor for aldose and aldehyde reductases. The hydrogen bonds between the active-site residues Tyr50, His113, and Trp114 and fidarestat are conserved in the two enzymes. In aldose reductase, Leu300 forms a hydrogen bond through its main-chain nitrogen atom with the exocyclic amide group of the inhibitor, which when replaced with a Pro in aldehyde reductase, cannot form a hydrogen bond, thus causing a loss in binding energy. Furthermore, in aldehyde reductase, the side chain of Trp220 occupies a disordered split conformation that is not observed in aldose reductase. Molecular modeling and inhibitory activity measurements suggest that the difference in the interaction between the side chain of Trp220 and fidarestat may contribute to the difference in the binding of the inhibitor to the enzymes.

Affiliations:

Australie, France, Japon, Suisse

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Le document en format XML

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<term>Complexe enzyme inhibiteur</term>
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<term>Modèle moléculaire</term>
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<term>Diffraction RX</term>
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<term>Modélisation</term>
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<term>Inhibiteur aldose reductase</term>
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<front><div type="abstract" xml:lang="en">Structure determination of porcine aldehyde reductase holoenzyme in complex with the potent aldose reductase inhibitor fidarestat was carried out to explain the difference in the potency of the inhibitor for aldose and aldehyde reductases. The hydrogen bonds between the active-site residues Tyr50, His113, and Trp114 and fidarestat are conserved in the two enzymes. In aldose reductase, Leu300 forms a hydrogen bond through its main-chain nitrogen atom with the exocyclic amide group of the inhibitor, which when replaced with a Pro in aldehyde reductase, cannot form a hydrogen bond, thus causing a loss in binding energy. Furthermore, in aldehyde reductase, the side chain of Trp220 occupies a disordered split conformation that is not observed in aldose reductase. Molecular modeling and inhibitory activity measurements suggest that the difference in the interaction between the side chain of Trp220 and fidarestat may contribute to the difference in the binding of the inhibitor to the enzymes.</div>
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Structure of aldehyde reductase holoenzyme in complex with the potent aldose reductase inhibitor fidarestat : Implications for inhibitor binding and selectivity

Structure of aldehyde reductase holoenzyme in complex with the potent aldose reductase inhibitor fidarestat : Implications for inhibitor binding and selectivity

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri