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Structural features of mammalian histidine decarboxylase reveal the basis for specific inhibition.

Moya-García, AA; Pino-Angeles, A; Gil-Redondo, R; Morreale, A; Sánchez-Jiménez, F; (2009) Structural features of mammalian histidine decarboxylase reveal the basis for specific inhibition. Br J Pharmacol , 157 (1) pp. 4-13. 10.1111/j.1476-5381.2009.00219.x.

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Abstract

For a long time the structural and molecular features of mammalian histidine decarboxylase (EC 4.1.1.22), the enzyme that produces histamine, have evaded characterization. We overcome the experimental problems for the study of this enzyme by using a computer-based modelling and simulation approach, and have now the conditions to use histidine decarboxylase as a target in histamine pharmacology. In this review, we present the recent (last 5 years) advances in the structure-function relationship of histidine decarboxylase and the strategy for the discovery of new drugs.

Type: Article
Title: Structural features of mammalian histidine decarboxylase reveal the basis for specific inhibition.
Location: England
DOI: 10.1111/j.1476-5381.2009.00219.x
Keywords: Animals, Binding Sites, Computer Simulation, Drug Design, Enzyme Inhibitors, Histidine Decarboxylase, Ligands, Models, Molecular, Molecular Structure, Structure-Activity Relationship, Thermodynamics
UCL classification: UCL > Provost and Vice Provost Offices
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Structural and Molecular Biology
URI: http://discovery.ucl.ac.uk/id/eprint/1432051
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