Structure based studies of the adaptive diversification process of congerins

Tsuyoshi Shirai, Clara Shionyu-Mitsuyama, Tomohisa Ogawa, Koji Muramoto

Research output: Contribution to journalReview articlepeer-review

5 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)567-573
Number of pages7
JournalMolecular Diversity
Issue number4
Publication statusPublished - 2006 Nov


  • Accelerated evolution
  • Bioinformatics
  • Crystal structure
  • Galectin


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