Abstract
The DOMIRE web server implements a novel, automatic, protein structural domain assignment procedure based on 3D substructures of the query protein which are also found within structures of a non-redundant protein database. These common 3D substructures are transformed into a co-occurrence matrix that offers a global view of the protein domain organization. Three different algorithms are employed to define structural domain boundaries from this co-occurrence matrix. For each query, a list of structural neighbors and their alignments are provided. DOMIRE, by displaying the protein structural domain organization, can be a useful tool for defining protein common cores and for unravelling the evolutionary relationship between different proteins. © The Author 2012. Published by Oxford University Press. All rights reserved.
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CITATION STYLE
Samson, F., Shrager, R., Tai, C. H., Sam, V., Lee, B., Munson, P. J., … Garnier, J. (2012). DOMIRE: A web server for identifying structural domains and their neighbors in proteins. Bioinformatics, 28(7), 1040–1041. https://doi.org/10.1093/bioinformatics/bts076
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