IIBBA   05544
INSTITUTO DE INVESTIGACIONES BIOQUIMICAS DE BUENOS AIRES
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
A NEW METHOD COMBINING MUTUAL INFORMATION AND CONSERVATION IMPROVES THE DETECTION OF CATALYTIC SITES IN PROTEINS
Autor/es:
ELIN TEPPA; DI DOMENICO TOMAS; MORTEN NIELSEN; CRISTINA MARINO BUSLE
Lugar:
Montevideo Uruguay
Reunión:
Congreso; International Sociey for Computational Biology (ISCB); 2010
Institución organizadora:
International Sociey for Computational Biology (ISCB)
Resumen:
.O {font-size:149%;} <!--.sld {left:0px !important; width:6.0in !important; height:8.66in !important; font-size:150% !important;} --> Catalytic residues (CR) play a fundamental role in enzymes and are generally expected to be conserved and located in the functional site of proteins. For this reason the conservation is the natural and intuitive way to predict functional residues. However many non-catalytic residues are highly conserved and not all catalytic residues are fully conserved throughout a given protein family. On the other hand, residues involved in coevolving residue networks have been postulated to be functionally important [1], and several studies have provided evidence that they are important for specificity or allosteric regulation [2-4]. Here, we put forward the hypothesis that CR carry a particular signature defined by networks of close proximity of residues with high mutual information (MI). This signature can be applied to differentiate functional from other non-functional conserved residues. The goal of this work is firstly validate the above hypothesis and demonstrate that functional residue are characterized by proximity residue networks of high mutual information, and secondly integrate this mutual information signature to create a method to identify catalytic residues and aid the locating the functional site of proteins.