Adaptive evolution of conger eel galectins

Ogawa Tomohisa; Shirai Tsuyoshi; Yamane Takashi; Kamiya Hisao; Muramoto Koji

doi:10.4052/tigg.14.177

Adaptive evolution of conger eel galectins

Ogawa Tomohisa, Shirai Tsuyoshi, Yamane Takashi, Kamiya Hisao, Muramoto Koji

AGR - Life Sciences

Research output: Contribution to journal › Short survey › peer-review

1 Citation (Scopus)

Abstract

Two galectins isolated from the skin mucus of conger eel (Conger myriaster), named congerins I and II, are dimers composed of two identical subunits of 136 and 135 amino acid residues, respectively. They belong to the proto-type galectins and showed 48% sequence identity and different thermal stabilities and different sugar binding. The molecular evolutionary analyses and X-ray crystallography analyses of congerins I and II reveal that they have evolved in an accelerating and adaptive manner to the emergence of a new structure including domain-swapping manner and a unique new ligand-binding site. In this review, we summarize and discuss the structure-properties/function relationships and the molecular evolution of fish galectins.

Original language	English
Pages (from-to)	177-187
Number of pages	11
Journal	Trends in Glycoscience and Glycotechnology
Volume	14
Issue number	77
DOIs	https://doi.org/10.4052/tigg.14.177
Publication status	Published - 2002 May

Keywords

Adaptive evolution
Conger eel
Domain swapping
Galectin
X-ray crystallography

ASJC Scopus subject areas

Biochemistry
Organic Chemistry

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10.4052/tigg.14.177

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title = "Adaptive evolution of conger eel galectins",

abstract = "Two galectins isolated from the skin mucus of conger eel (Conger myriaster), named congerins I and II, are dimers composed of two identical subunits of 136 and 135 amino acid residues, respectively. They belong to the proto-type galectins and showed 48% sequence identity and different thermal stabilities and different sugar binding. The molecular evolutionary analyses and X-ray crystallography analyses of congerins I and II reveal that they have evolved in an accelerating and adaptive manner to the emergence of a new structure including domain-swapping manner and a unique new ligand-binding site. In this review, we summarize and discuss the structure-properties/function relationships and the molecular evolution of fish galectins.",

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author = "Ogawa Tomohisa and Shirai Tsuyoshi and Yamane Takashi and Kamiya Hisao and Muramoto Koji",

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T1 - Adaptive evolution of conger eel galectins

AU - Tomohisa, Ogawa

AU - Tsuyoshi, Shirai

AU - Takashi, Yamane

AU - Hisao, Kamiya

AU - Koji, Muramoto

PY - 2002/5

Y1 - 2002/5

N2 - Two galectins isolated from the skin mucus of conger eel (Conger myriaster), named congerins I and II, are dimers composed of two identical subunits of 136 and 135 amino acid residues, respectively. They belong to the proto-type galectins and showed 48% sequence identity and different thermal stabilities and different sugar binding. The molecular evolutionary analyses and X-ray crystallography analyses of congerins I and II reveal that they have evolved in an accelerating and adaptive manner to the emergence of a new structure including domain-swapping manner and a unique new ligand-binding site. In this review, we summarize and discuss the structure-properties/function relationships and the molecular evolution of fish galectins.

AB - Two galectins isolated from the skin mucus of conger eel (Conger myriaster), named congerins I and II, are dimers composed of two identical subunits of 136 and 135 amino acid residues, respectively. They belong to the proto-type galectins and showed 48% sequence identity and different thermal stabilities and different sugar binding. The molecular evolutionary analyses and X-ray crystallography analyses of congerins I and II reveal that they have evolved in an accelerating and adaptive manner to the emergence of a new structure including domain-swapping manner and a unique new ligand-binding site. In this review, we summarize and discuss the structure-properties/function relationships and the molecular evolution of fish galectins.

KW - Adaptive evolution

KW - Conger eel

KW - Domain swapping

KW - Galectin

KW - X-ray crystallography

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