Insights into Evolution of Calcium-Binding Proteins
Author Information
Author(s): Rigden Daniel J., Woodhead Duncan D., Wong Prudence W. H., Galperin Michael Y.
Primary Institution: Institute of Integrative Biology, University of Liverpool
Hypothesis
How did the Dx[DN]xDG calcium-binding motif arise in various protein folds?
Conclusion
The study reveals new structural contexts for the Dx[DN]xDG motif, suggesting its convergent evolution across different proteins.
Supporting Evidence
- The study identified four new structural contexts for the Dx[DN]xDG motif.
- Calcium binding was observed in all new examples except one, where manganese was bound instead.
- The analysis suggests a common evolutionary origin for the calcium-binding motifs across different proteins.
- Calcium-binding motifs are often found in proteins that are secreted or localized to the cell surface.
Takeaway
This study found that a special pattern in proteins helps them bind calcium, which is important for their function, and this pattern has evolved in many different proteins.
Methodology
The researchers analyzed various protein structures to identify new instances of the Dx[DN]xDG motif and its evolutionary implications.
Limitations
The study may not cover all possible structural contexts for the motif due to the limitations of current protein databases.
Digital Object Identifier (DOI)
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