Database of protein conformational diversity explained

The Database of protein conformational diversity (PCDB) is a database of diversity of protein tertiary structures within protein domains as determined by X-ray crystallography.^{[1] [2]} Proteins are inherently flexible and this database collects information on this subject for use in molecular research. It uses the CATH database as a source of structures for each protein and reports the range of differences in the structures based on their superposition and reports a maximum RMSD. The interface for the database allows researchers to find proteins with a range of conformational flexibility allowing them to find highly flexible proteins for example. The database is run and maintained by a group of researchers based at the Universidad Nacional de Quilmes in Argentina.

See also

• Crystallography
• Protein structure

External links

• Web site: Protein Conformational Database . Juritz, Ezequiel Iván . Fernández Alberti, Sebastián . Parisi, Gustavo Danie . Structural Bioinformatics Group; National University of Quilmes . 2011-08-19 . dead . https://web.archive.org/web/20120330231747/http://74.54.147.134/~ezepcdb3/ . 2012-03-30 .

Notes and References

1. Juritz EI, Alberti SF, Parisi GD . PCDB: a database of protein conformational diversity . Nucleic Acids Res. . 39 . Database issue . D475–9 . January 2011 . 21097895 . 3013735 . 10.1093/nar/gkq1181 .
2. Galperin MY, Cochrane GR . The 2011 Nucleic Acids Research Database Issue and the online Molecular Biology Database Collection . Nucleic Acids Res. . 39 . Database issue . D1–6 . January 2011 . 21177655 . 3013748 . 10.1093/nar/gkq1243 .