Identification of the amino acid residue in the nematode galectin LEC-1 responsible for its unique sugar binding property: analysis by combination of site-directed mutagenesis and frontal affinity chromatography.

Identification of the amino acid residue in the nematode galectin LEC-1 responsible for its unique sugar binding property: analysis by combination of site-directed mutagenesis and frontal affinity chromatography. Research Abstract Details 

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Identification of the amino acid residue in the nematode galectin LEC-1 responsible for its unique sugar binding property: analysis by combination of site-directed mutagenesis and frontal affinity chromatography. Abstract Text:

Yoichiro Arata,Norihide Ishii,Mayumi Tamura,Takamasa Nonaka,Ken-ichi Kasai,Yoichiro Arata,Norihide Ishii,Mayumi Tamura,Takamasa Nonaka,Ken-ichi Kasai,

The basic disaccharide structure recognized by galectin family members is the lactosamine-like structure Galbeta1-4(3)Glc(NAc). In galectins, eight highly conserved amino acid residues participate in the recognition of this basic structure. Each galectin seems to mediate diverse biological functions due to recognition of different modifications of the basic disaccharide Galbeta1-4(3)Glc(NAc), but there is very little information about which amino acid residue in galectin is responsible for recognizing these modifications. The 32-kDa galectin LEC-1 of the nematode Caenorhabditis elegans is composed of two domains, each of which is homologous to vertebrate 14-kDa-type galectins. Although both lectin domains have an affinity for N-acetyllactosamine (Galbeta1-4GlcNAc)-containing, N-linked, complex-type sugar chains, the N-terminal lectin domain of LEC-1 recognizes blood group A saccharide (GalNAcalpha1-3(Fucalpha1-2)Galbeta1-3GlcNAc), whereas this saccharide is only poorly recognized by the C-terminal domain. Here, we used a combination of site-directed mutagenesis of the N-terminal lectin domain of galectin LEC-1 and an analysis of the sugar-binding profile by frontal affinity chromatography to identify the amino acid residues important for this recognition. Our results indicate that Thr(41) in the N-terminal lectin domain of LEC-1 is important for its affinity for A-hexasaccharide.

Identification of the amino acid residue in the nematode galectin LEC-1 responsible for its unique sugar binding property: analysis by combination of site-directed mutagenesis and frontal affinity chromatography. Publishing Authors By Initials

Y Arata,N Ishii,M Tamura,T Nonaka,K Kasai,Y Arata,N Ishii,M Tamura,T Nonaka,K Kasai,

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Identification of the amino acid residue in the nematode galectin LEC-1 responsible for its unique sugar binding property: analysis by combination of site-directed mutagenesis and frontal affinity chromatography. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Biological & pharmaceutical bulletin

VOLUME: 30

Page Numbers: 2012-7

Journal Abbreviation: Biol. Pharm. Bull.

ISSN: 0918-6158

DAY: 5

MONTH: Nov

YEAR: 2007

Identification of the amino acid residue in the nematode galectin LEC-1 responsible for its unique sugar binding property: analysis by combination of site-directed mutagenesis and frontal affinity chromatography. Information

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LANGUAGE: eng

NlmUniqueID: 9311984

Identification of the amino acid residue in the nematode galectin LEC-1 responsible for its unique sugar binding property: analysis by combination of site-directed mutagenesis and frontal affinity chromatography. Keywords Mesh Terms:

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Grant and Affiliation Information for Identification of the amino acid residue in the nematode galectin LEC-1 responsible for its unique sugar binding property: analysis by combination of site-directed mutagenesis and frontal affinity chromatography.

AFFILIATION: Department of Biological Chemistry, Teikyo University School of Pharmaceutical Sciences, Sagamiko, Kanagawa, Japan. arata@josai.ac.jp

Country: Japan

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MEDLINETA: Biol Pharm Bull

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