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

研究成果: ジャーナルへの寄稿記事

116 引用 (Scopus)

抄録

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.

元の言語英語
ページ(範囲)17929-17932
ページ数4
ジャーナルJournal of Biological Chemistry
275
発行部数24
DOI
出版物ステータス出版済み - 6 16 2000
外部発表Yes

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Chitin
Invertebrates
Carrier Proteins
Horseshoe Crabs
Hemocytes
Nuclear magnetic resonance spectroscopy
Magnetic Resonance Spectroscopy
Peptides

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

これを引用

Chitin-binding proteins in invertebrates and plants comprise a common chitin-binding structural motif. / Suetake, Tetsuya; Tsuda, Sakae; Kawabata, Shun-Ichiro; Miura, Kazunori; Iwanaga, Sadaaki; Hikichi, Kunio; Nitta, Katsutoshi; Kawano, Keiichi.

:: Journal of Biological Chemistry, 巻 275, 番号 24, 16.06.2000, p. 17929-17932.

研究成果: ジャーナルへの寄稿記事

Suetake, T, Tsuda, S, Kawabata, S-I, Miura, K, Iwanaga, S, Hikichi, K, Nitta, K & Kawano, K 2000, 'Chitin-binding proteins in invertebrates and plants comprise a common chitin-binding structural motif', Journal of Biological Chemistry, 巻. 275, 番号 24, pp. 17929-17932. https://doi.org/10.1074/jbc.C000184200
Suetake, Tetsuya ; Tsuda, Sakae ; Kawabata, Shun-Ichiro ; Miura, Kazunori ; Iwanaga, Sadaaki ; Hikichi, Kunio ; Nitta, Katsutoshi ; Kawano, Keiichi. / Chitin-binding proteins in invertebrates and plants comprise a common chitin-binding structural motif. :: Journal of Biological Chemistry. 2000 ; 巻 275, 番号 24. pp. 17929-17932.
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abstract = "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.",
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AU - Tsuda, Sakae

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AU - Miura, Kazunori

AU - Iwanaga, Sadaaki

AU - Hikichi, Kunio

AU - Nitta, Katsutoshi

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