INVESTIGADORES
FERNANDEZ Pablo Mariano
congresos y reuniones científicas
Título:
Proteomics of Arginine Kinase (AK) from T. cruzi : Three-dimensional X-Ray Structure at 2.0 Å Resolution
Autor/es:
PABLO FERNANDEZ; P ALZARI; C PEREIRA; C AGUILAR
Lugar:
Merlo, San Luis
Reunión:
Encuentro; XXII Reunión Anual de la Sociedad de Biología de Cuyo; 2004
Resumen:
Arginine kinase buffers cellular ATP levels by catalysing reversible phosphoryl transfer between ATP and arginine. Trypanosoma cruzi arginine kinase is not present in mammalian tissues, making it a suitable target for rational drug design of chemotherapeutic agents against Chagas disease and other parasitic diseases caused by related organisms such as T. brucei The structure at 2.0 Å of the native apo-enzyme refined to an R-factor of 0.23 including about 200 water molecules. The enzyme has 357 residues which build into two domains. Domain 1 belong to the alpha class with an orthogonal bundle architecture. Domain 2 is an Alpha Beta 2-layer sandwich.
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