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Nucleic Acids Research 2006 34(Database Issue):D281-D284; doi:10.1093/nar/gkj057
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Nucleic Acids Research, 2006, Vol. 34, Database issue D281-D284
© The Author 2006. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oxfordjournals.org


Article

Gene3D: modelling protein structure, function and evolution

Corin Yeats*, Michael Maibaum, Russell Marsden, Mark Dibley, David Lee, Sarah Addou and Christine A. Orengo

Department of Biochemistry and Molecular Biology, University College London Gower Street, London, WC1E 6BT, UK

*To whom correspondence should be addressed. Tel: +44 20 7679 3890; Fax: +44 20 7679 7193; Email: yeats{at}biochem.ucl.ac.uk

Received September 15, 2005. Accepted October 4, 2005.

The Gene3D release 4 database and web portal (http://cathwww.biochem.ucl.ac.uk:8080/Gene3D) provide a combined structural, functional and evolutionary view of the protein world. It is focussed on providing structural annotation for protein sequences without structural representatives—including the complete proteome sets of over 240 different species. The protein sequences have also been clustered into whole-chain families so as to aid functional prediction. The structural annotation is generated using HMM models based on the CATH domain families; CATH is a repository for manually deduced protein domains. Amongst the changes from the last publication are: the addition of over 100 genomes and the UniProt sequence database, domain data from Pfam, metabolic pathway and functional data from COGs, KEGG and GO, and protein–protein interaction data from MINT and BIND. The website has been rebuilt to allow more sophisticated querying and the data returned is presented in a clearer format with greater functionality. Furthermore, all data can be downloaded in a simple XML format, allowing users to carry out complex investigations at their own computers.


The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors


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