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Crystal structure of GABA-aminotransferase, a target for antiepileptic drug therapy

Storici, P. and Capitani, G. and De Biase, D. and Moser, M. and John, R. A. and Jansonius, J. N. and Schirmer, T.. (1999) Crystal structure of GABA-aminotransferase, a target for antiepileptic drug therapy. Biochemistry, 38 (27). pp. 8628-8634.

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Abstract

gamma-Aminobutyrate aminotransferase (GABA-AT), a pyridoxal phosphate-dependent enzyme, is responsible for the degradation of the inhibitory neurotransmitter GABA and is a target for antiepileptic drugs because its selective inhibition raises GABA concentrations in brain. The X-ray structure of pig GABA-AT has been determined to 3.0 A resolution by molecular replacement with the distantly related enzyme ornithine aminotransferase. Both omega-aminotransferases have the same fold, but exhibit side chain replacements in the closely packed binding site that explain their respective specificities. The aldimines of GABA and the antiepileptic drug vinyl-GABA have been modeled into the active site.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Schirmer)
UniBasel Contributors:Schirmer, Tilman
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:American Chemical Society
ISSN:0006-2960
Note:Publication type according to Uni Basel Research Database: Journal article
Language:English
Identification Number:
Last Modified:10 Aug 2018 14:03
Deposited On:22 Mar 2012 13:20

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