Homology Modeling and Blind Docking Approach Studies of Pig Heart Fumarase
The fumarase is an enzyme that could be used as target indrug design to treat infections by Helicobacter pylori andTrypanosoma brucei. In the first step, homology modeling wasemployed to build the 3D structure of pig heart fumarase (FUM P).Then, Q-Site Finder program was used to identify the potenti...
| Autores: | , , |
|---|---|
| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2007 |
| País: | México |
| Institución: | Instituto Politécnico Nacional |
| Repositorio: | Redalyc-IPN |
| OAI Identifier: | oai:redalyc.org:47551305 |
| Acceso en línea: | https://www.redalyc.org/articulo.oa?id=47551305 |
| Access Level: | acceso abierto |
| Palabra clave: | Multidisciplinaria (Ciencias Naturales y Exactas) docking Homology arylderivatives pig heart fumarase |
| Sumario: | The fumarase is an enzyme that could be used as target indrug design to treat infections by Helicobacter pylori andTrypanosoma brucei. In the first step, homology modeling wasemployed to build the 3D structure of pig heart fumarase (FUM P).Then, Q-Site Finder program was used to identify the potential bindingsites of FUM P and fumarase of Saccharomyces cerevisiae (FUMY). Further, molecular docking of arylderivatives substituted at thearomatic ring with an electron withdrawing or donating groups wereevaluated on FUM P and on FUM Y to validate the homology model.The homology model of FUM P showed a structure very similar(70.33 % of identity in sequence) to the crystal structure of FUM Y.Some active sites were identified by Q-Site Finder server on FUM Pand on FUM Y which could correspond to sites A and B. The dockingresults showed that some compounds were bonded at the site Aon FUM P and FUM Y being those with electron withdrawing groupswith more affinity on FUM P, suggesting that electronic effects arethe more important ones during the recognition process by FUM P. |
|---|