http://www.cnr.it/ontology/cnr/individuo/prodotto/ID269536
Structural basis for the rational design of new anti-Brucella agents: The crystal structure of the C366S mutant of l-histidinol dehydrogenase from Brucella suis. (Articolo in rivista)
- Type
- Label
- Structural basis for the rational design of new anti-Brucella agents: The crystal structure of the C366S mutant of l-histidinol dehydrogenase from Brucella suis. (Articolo in rivista) (literal)
- Anno
- 2014-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/j.biochi.2013.09.028 (literal)
- Alternative label
D'ambrosio K, Lopez M, Dathan NA, Ouahrani-Bettache S, Köhler S, Ascione G, Monti SM, Winum JY, De Simone G. (2014)
Structural basis for the rational design of new anti-Brucella agents: The crystal structure of the C366S mutant of l-histidinol dehydrogenase from Brucella suis.
in Biochimie (Print); Elsevier, Amsterdam (Paesi Bassi)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- D'ambrosio K, Lopez M, Dathan NA, Ouahrani-Bettache S, Köhler S, Ascione G, Monti SM, Winum JY, De Simone G. (literal)
- Rivista
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- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Istituto di Biostrutture e Bioimmagini-CNR, Via Mezzocannone 16, 80134 Napoli, Italy
Institut des Biomolécules Max Mousseron (IBMM), UMR 5247 CNRS-UM1-UM2, Bâtiment de Recherche Max Mousseron, Ecole Nationale Supérieure de Chimie de Montpellier, 8 rue de l'Ecole Normale, 34296 Montpellier Cedex, France
Centre d'Etudes d'Agents Pathogènes et Biotechnologies pour la Santé (CPBS), UMR 5236 CNRS-UM1-UM2, 1919 Route de Mende, 34293 Montpellier, France (literal)
- Titolo
- Structural basis for the rational design of new anti-Brucella agents: The crystal structure of the C366S mutant of l-histidinol dehydrogenase from Brucella suis. (literal)
- Abstract
- l-Histidinol dehydrogenase from Brucella suis (BsHDH) is an enzyme involved in the histidine biosynthesis pathway which is absent in mammals, thus representing a very interesting target for the development of anti-Brucella agents. In this paper we report the crystallographic structure of a mutated form of BsHDH both in its unbound form and in complex with a nanomolar inhibitor. These studies provide the first structural background for the rational design of potent HDH inhibitors, thus offering new hints for clinical applications. (literal)
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