| Literature DB >> 22345617 |
Franck Samson1, Richard Shrager, Chin-Hsien Tai, Vichetra Sam, Byungkook Lee, Peter J Munson, Jean-François Gibrat, Jean Garnier.
Abstract
SUMMARY: 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. AVAILABILITY: http://genome.jouy.inra.fr/domire CONTACT: jean.garnier@jouy.inra.fr.Mesh:
Substances:
Year: 2012 PMID: 22345617 PMCID: PMC3315711 DOI: 10.1093/bioinformatics/bts076
Source DB: PubMed Journal: Bioinformatics ISSN: 1367-4803 Impact factor: 6.937