CPDB: a database of circular permutation in proteins

Circular permutation (CP) in a protein can be considered as if its sequence were circularized followed by a creation of termini at a new location. Since the first observation of CP in 1979, a substantial number of studies have concluded that circular permutants (CPs) usually retain native structures...

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Bibliographic Details
Published in:Nucleic acids research 2009-01, Vol.37 (suppl-1), p.D328-D332
Main Authors: Lo, Wei-Cheng, Lee, Chi-Ching, Lee, Che-Yu, Lyu, Ping-Chiang
Format: Article
Language:English
Subjects:
Computer Graphics
Databases, Protein
Internet
Protein Folding
Proteins - chemistry
Structural Homology, Protein
User-Computer Interface
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Summary:Circular permutation (CP) in a protein can be considered as if its sequence were circularized followed by a creation of termini at a new location. Since the first observation of CP in 1979, a substantial number of studies have concluded that circular permutants (CPs) usually retain native structures and functions, sometimes with increased stability or functional diversity. Although this interesting property has made CP useful in many protein engineering and folding researches, large-scale collections of CP-related information were not available until this study. Here we describe CPDB, the first CP DataBase. The organizational principle of CPDB is a hierarchical categorization in which pairs of circular permutants are grouped into CP clusters, which are further grouped into folds and in turn classes. Additions to CPDB include a useful set of tools and resources for the identification, characterization, comparison and visualization of CP. Besides, several viable CP site prediction methods are implemented and assessed in CPDB. This database can be useful in protein folding and evolution studies, the discovery of novel protein structural and functional relationships, and facilitating the production of new CPs with unique biotechnical or industrial interests. The CPDB database can be accessed at http://sarst.life.nthu.edu.tw/cpdb
ISSN:0305-1048
1362-4962
DOI:10.1093/nar/gkn679