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Protein-protein and protein-ligand interactions govern almost all biological phenomena, and analyses at an atomic level have been performed to reveal the precise mechanisms for individual specific recognitions at protein interfaces.For the former [1] and the latter interactions [2], we performed exhaustive all-against-all atomic structure comparisons of all known binding sites, and identified recurring elementary motifs.By integrating the elementary motifs associated with each protein subunit, we defined composite motifs, from which function similarity can be better inferred [3].