Literature DB >> 14681397

E-MSD: an integrated data resource for bioinformatics.

A Golovin1, T J Oldfield, J G Tate, S Velankar, G J Barton, H Boutselakis, D Dimitropoulos, J Fillon, A Hussain, J M C Ionides, M John, P A Keller, E Krissinel, P McNeil, A Naim, R Newman, A Pajon, J Pineda, A Rachedi, J Copeland, A Sitnov, S Sobhany, A Suarez-Uruena, G J Swaminathan, M Tagari, S Tromm, W Vranken, K Henrick.   

Abstract

The Macromolecular Structure Database (MSD) group (http://www.ebi.ac.uk/msd/) continues to enhance the quality and consistency of macromolecular structure data in the Protein Data Bank (PDB) and to work towards the integration of various bioinformatics data resources. We have implemented a simple form-based interface that allows users to query the MSD directly. The MSD 'atlas pages' show all of the information in the MSD for a particular PDB entry. The group has designed new search interfaces aimed at specific areas of interest, such as the environment of ligands and the secondary structures of proteins. We have also implemented a novel search interface that begins to integrate separate MSD search services in a single graphical tool. We have worked closely with collaborators to build a new visualization tool that can present both structure and sequence data in a unified interface, and this data viewer is now used throughout the MSD services for the visualization and presentation of search results. Examples showcasing the functionality and power of these tools are available from tutorial webpages (http://www. ebi.ac.uk/msd-srv/docs/roadshow_tutorial/).

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Year:  2004        PMID: 14681397      PMCID: PMC308812          DOI: 10.1093/nar/gkh078

Source DB:  PubMed          Journal:  Nucleic Acids Res        ISSN: 0305-1048            Impact factor:   16.971


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10.  The Pfam protein families database.

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8.  Structural fragment clustering reveals novel structural and functional motifs in alpha-helical transmembrane proteins.

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9.  Analysis of proteins with the 'hot dog' fold: prediction of function and identification of catalytic residues of hypothetical proteins.

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