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Issue 25, 2017
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Elucidation of inhibitor-binding pockets of D-amino acid oxidase using docking simulation and N-sulfanylethylanilide-based labeling technology

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Abstract

Because of the relevance of D-serine (D-Ser) to schizophrenia, inhibitors of D-amino acid oxidase (DAO), which catalyzes degradation of D-Ser in the presence of flavin adenine dinucleotide (FAD), are expected to be anti-schizophrenia therapeutics. In this study, binding pockets of DAO to its inhibitor 4-bromo-3-nitrobenzoic acid were searched by combining in silico docking simulation and labeling experiments employing an N-sulfanylethylanilide-based labeling technology that we have developed. The results clearly demonstrated that there are two binding pockets: one is shared with D-Ser and FAD, and the other is an unexpected cleft between the subunits of a DAO dimer. These findings will provide insight to aid the development of new DAO inhibitors. In addition, it was also proved that our labeling technology could be applicable to elucidate the binding pockets of proteins.

Graphical abstract: Elucidation of inhibitor-binding pockets of d-amino acid oxidase using docking simulation and N-sulfanylethylanilide-based labeling technology

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Publication details

The article was received on 15 Mar 2017, accepted on 05 May 2017 and first published on 05 May 2017


Article type: Paper
DOI: 10.1039/C7OB00633K
Citation: Org. Biomol. Chem., 2017,15, 5289-5297
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    Elucidation of inhibitor-binding pockets of D-amino acid oxidase using docking simulation and N-sulfanylethylanilide-based labeling technology

    T. Kohiki, Y. Kato, Y. Nishikawa, K. Yorita, I. Sagawa, M. Denda, T. Inokuma, A. Shigenaga, K. Fukui and A. Otaka, Org. Biomol. Chem., 2017, 15, 5289
    DOI: 10.1039/C7OB00633K

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