New opportunities for protease ligand-binding site comparisons using SitesBase.
The rapid expansion of structural information for protein ligand-binding sites is potentially an important source of information in structure-based drug design and in understanding ligand cross-reactivity and toxicity. We have developed SitesBase, a comprehensive database of ligand-binding sites extracted automatically from the Macromolecular Structure Database. SitesBase is an easily accessible database which is simple to use and holds pre-calculated information about structural similarities between known ligand-binding sites. These similarities are presented to the wider community enabling binding-site comparisons for therapeutically interesting protein families, such as the proteases and for new proteins to enable the discovery of interesting new structure-function relationships. The database is available from http://www.modelling.leeds.ac.uk/sb/.
Gold
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ND
Institute of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, UK.
Deville
K
K
Jackson
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RM
D000818:Animals; D001665:Binding Sites; D020134:Catalytic Domain; D030562:Databases, Protein; D006801:Humans; D008024:Ligands; D046911:Macromolecular Substances; D008958:Models, Molecular; D010447:Peptide Hydrolases / Q000737:chemistry* / Q000378:metabolism*; D011494:Protein Kinases / Q000737:chemistry / Q000378:metabolism; D020860:Subtilisin / Q000737:chemistry / Q000378:metabolism; D014357:Trypsin / Q000737:chemistry / Q000378:metabolism
D008024:Ligands; D046911:Macromolecular Substances; D011494:Protein Kinases; D010447:Peptide Hydrolases; D014357:Trypsin; D020860:Subtilisin