Comparación de la Estructura, Dinámica y Propiedades de Interacción con Carbohidratos de las Galectinas Humanas

CARLOS M. A. GUARDIA; DIEGO GAUTO; SANTIAGO DI LELLA; GABRIEL RABINOVICH; MARCELO MARTI; DARÍO A. ESTRIN

Quilmes

Congreso; 1er Congreso Argentino de Bioinformática y Biología Computacional; 2010

Asociación Argentina de Bioinformática y Biología Computacional

Galectins constitute a family of multi-functional lectin proteins extensively distributed in a variety of tissues and animal species. They are defined by their specificity for b-galactoside sugars and consensus sequence in the carbohydrate recognition domain (CRD). Although all the galectins have a highly homologous CRD, small differences in their binding specificity have been observed which are functionally relevant. The structural basis for these fine tuning is unknown. In humans 15 different galectin sequences have been detected and only seven of them have been structurally characterized. Furthermore, neither a global comparison nor one of the individual monosaccharide binding sites across the whole protein family has been performed. To bridge this gap, we have performed a structural-dynamical comparison of all human members of the galectin family using state of the art computer simulation techniques.