Chitin-binding proteins in invertebrates and plants comprise a common chitin-binding structural motif

Tetsuya Suetake, Sakae Tsuda, Shun Ichiro Kawabata, Kazunori Miura, Sadaaki Iwanaga, Kunio Hikichi, Katsutoshi Nitta, Keiichi Kawano

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123 Citations (Scopus)


Tachycitin, a 73-residue polypeptide having antimicrobial activity is present in the hemocyte of horseshoe crab (Tachypleus tridentatus). The first three-dimensional structure of invertebrate chitin-binding protein was determined for tachycitin using two-dimensional nuclear magnetic resonance spectroscopy. The measurements indicate that the structure of tachycitin is largely divided into N- and C-terminal domains; the former comprises a three- stranded β-sheet and the latter a two-stranded β-sheet following a short helical turn. The latter structural motif shares a significant tertiary structural similarity with the chitin-binding domain of plant chitin-binding protein. This result is thought to provide faithful experimental evidence to the recent hypothesis that chitin-binding proteins of invertebrates and plants are correlated by a convergent evolution process.

Original languageEnglish
Pages (from-to)17929-17932
Number of pages4
JournalJournal of Biological Chemistry
Issue number24
Publication statusPublished - Jun 16 2000
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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