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Protein Engineering, Vol. 13, No. 3, 153-165, March 2000
© 2000 Oxford University Press

The CATH Dictionary of Homologous Superfamilies (DHS): a consensus approach for identifying distant structural homologues

J.E. Bray1,2, A.E. Todd1, F.M.G. Pearl1, J.M. Thornton1,3 and C.A. Orengo1

1 Biomolecular Structure and Modelling Unit, Department of Biochemistry and Molecular Biology, University College London, Gower Street,London WC1E 6BT, UK, 3 Department of Crystallography, Birkbeck College, Malet Street, London WC1E 7HX, UK

A consensus approach has been developed for identifying distant structural homologues. This is based on the CATH Dictionary of Homologous Superfamilies (DHS), a database of validated multiple structural alignments annotated with consensus functional information for evolutionary protein superfamilies (URL: http://www.biochem.ucl.ac.uk/bsm/dhs). Multiple structural alignments have been generated for 362 well-populated superfamilies in the CATH structural domain database and annotated with secondary structure, physicochemical properties, functional sequence patterns and protein–ligand interaction data. Consensus functional information for each superfamily includes descriptions and keywords extracted from SWISS-PROT and the ENZYME database. The Dictionary provides a powerful resource to validate, examine and visualize key structural and functional features of each homologous superfamily. The value of the DHS, for assessing functional variability and identifying distant evolutionary relationships, is illustrated using the pyridoxal-5'-phosphate (PLP) binding aspartate aminotransferase superfamily. The DHS also provides a tool for examining sequence–structure relationships for proteins within each fold group.


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