INQUIMAE   12526
INSTITUTO DE QUIMICA, FISICA DE LOS MATERIALES, MEDIOAMBIENTE Y ENERGIA
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Aromatic-Aromatic interactions in proteins: beyond the dimer.
Autor/es:
ESTEBAN LANZAROTTI; MARCELO MARTI; A.G. TURJANSKI
Lugar:
Quilmes, Buenos Aires
Reunión:
Congreso; Primer Congreso Sociead Argentina de Bioinformatica y Biologia Computacional; 2010
Institución organizadora:
Sociedad Argnetina de Bioinformatica y Biologia Computacional
Resumen:
Aromatic residues are key widespread elements of protein structures, and have been shown to be important for structure stability, folding, protein-protein recognition and ligand binding. The pair-pair interaction of aromatic residues in the context of protein structures has been extensively studied. On the other hand, it is well known that isolated aromatic molecules tend to form higher order clusters, beyond the dimer, with specific spatial conformations. However, to the best of our knowledge no characterization and/or classification of clusters of aromatic residues in proteins have been provided so far. To bridge the gap, we have surveyed protein structures deposited in the PDB and identified and characterized higher order clusters formed by aromatic aminoacids. Our results show that higher order aromatic clusters exist in a big subset of the proteins crystallized so far. We found that aromatic trimers and tetramers are the basic units of aromatic clusters. Interestingly, timers and tetramers adopt specific conformations which resemble the most favorable conformation observed in isolated benzene clusters, indicating that proteins seem to have been optimized by evolution to have the best possible interactions among aromatic aminoacids in protein folds. We show an example of a protein family, calmodulin like, that have a conserved trimer important for protein stability and ligand recognition. The identification and classification of aromatic clusters presented in our work allows a better understanding of protein structure, folding and interactions and will help to identify these important motifs in protein families to link them to specific protein functions
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