Summary
The isoforms of a fish galectin, congerins I and II, have several features that make them suitable for a study of accelerated process of molecular diversification based on 3D structures: They have been generated by a gene duplication, and still maintain 47% amino acid sequence identity to each other. Their genes show very high K A/K S ratio, and are though to be components of fish defense system. The crystal systems for a high-resolution analysis are known for both proteins. A series of works with biochemistry, molecular biology, and X-ray crystallography techniques have suggested that the two proteins might have evolved under differential selection pressures. Congerin I appeared to be a stabilized version of galectin-1. Congerin II was shown to be adapted to a new carbohydrate-ligand. The 3D structures of the wild type and mutant proteins have revealed the probable cause and consequence of the selection pressure responsible for the diversification of congerins.
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Abbreviations
- 3D:
-
three dimensional
- MES:
-
2-N-morpholino ethane sulfonic acid
- PDB:
-
protein data bank
- ML:
-
maximum likelihood
- MP:
-
maximum parsimony
- SE:
-
standard error
- PCR:
-
polymerase chain reaction
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Shirai, T., Shionyu-Mitsuyama, C., Ogawa, T. et al. Structure based studies of the adaptive diversification process of congerins. Mol Divers 10, 567–573 (2006). https://doi.org/10.1007/s11030-006-9030-8
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DOI: https://doi.org/10.1007/s11030-006-9030-8