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.[citation needed]
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| Content | |
|---|---|
| Description | Protein conformational diversity. |
| Contact | |
| Research center | Universidad Nacional de Quilmes |
| Laboratory | Centro de Estudios e Investigaciones |
| Authors | Ezequiel I Juritz |
| Primary citation | Juritz & al. (2011)[1] |
| Release date | 2010 |
| Access | |
| Website | http://www.pcdb.unq.edu.ar |
See also
editReferences
edit- ^ a b Juritz EI, Alberti SF, Parisi GD (January 2011). "PCDB: a database of protein conformational diversity". Nucleic Acids Res. 39 (Database issue): D475–9. doi:10.1093/nar/gkq1181. PMC 3013735. PMID 21097895.
- ^ Galperin MY, Cochrane GR (January 2011). "The 2011 Nucleic Acids Research Database Issue and the online Molecular Biology Database Collection". Nucleic Acids Res. 39 (Database issue): D1–6. doi:10.1093/nar/gkq1243. PMC 3013748. PMID 21177655.
External links
edit- Juritz, Ezequiel Iván; Fernández Alberti, Sebastián; Parisi, Gustavo Danie. "Protein Conformational Database". Structural Bioinformatics Group; National University of Quilmes. Archived from the original on 2012-03-30. Retrieved 2011-08-19.
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