Automatic determination and classification of structural domains of proteins and development of interaction database

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We have conducted exhaustive comparison and classification of interaction interface structures in proteins the result of which is summarized as a list of structural motifs. In particular, we have found that the structural motifs for protein binding interfaces are shared only among homologous proteins. This suggested structural motifs may better correspond to protein functions compared to traditional approaches based on overall folds. Furthermore, we have defined" composite motifs" by grouping together the individual structural motifs present in each subunit and studied the correlation between such composite motifs and biological functions. It was found that the composite motifs had more robust correlation with function than bare structural similarities of interfaces or sequence similarity.