Internal symmetry in protein structures: prevalence, functional relevance and evolution
1MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, United Kingdom.
Current Opinion in Structural Biology
|June 21, 2015
Summary
Internal symmetry is prevalent in protein structures, with about 20% of known protein folds exhibiting this characteristic. Understanding protein symmetry is key to deciphering protein functions and structural integrity.
Area of Science:
- Structural biology
- Bioinformatics
- Evolutionary biology
Background:
- Symmetry is observed across biological organization levels, particularly in protein structures.
- Evolutionary studies suggest links between internal protein symmetry, quaternary structure, and function.
- Computational tools like SymD and CE-Symm enable large-scale symmetry detection.
Purpose of the Study:
- To investigate the prevalence and implications of internal symmetry in protein structures.
- To explore the relationship between protein symmetry, structural integrity, and biological function.
Main Methods:
- Utilized computational methods (SymD, CE-Symm) for large-scale detection of internal symmetry in protein structures.
- Analyzed data from the Structural Classification of Proteins (SCOP) database.
Main Results:
- Approximately 20% of SCOP folds, superfamilies, and families show internal symmetry.
- All-beta and membrane protein classes exhibit a higher frequency of internal symmetry.
- Regions connecting symmetric units may correlate with functionally important sites.
Conclusions:
- Internal symmetry is a significant feature in a substantial portion of protein structures.
- Further research is needed to establish general principles governing protein internal symmetry and its functional relevance.
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