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erythrina corallodendron/carbohydrate
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Faqja 1 nga 30 rezultatet
Defining the carbohydrate specificities of Erythrina corallodendron lectin (ECorL) as polyvalent Galbeta1-4GlcNAc (II) > monomeric II > monomeric Gal and GalNAc.
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Identifikohuni Regjistrohu
BACKGROUND
Erythrina corallodendron lectin (ECorL) is one of the potent applied lectins. In previous studies, the carbohydrate specificities of this lectin were limited to monosaccharides, simple oligosaccharides and several clusters. However, the polyvalent factor has not been
Differences in the cross-linking activities of native and recombinant Erythrina corallodendron lectin with asialofetuin. Evidence for carbohydrate-carbohydrate interactions in lectin-glycoprotein complexes.
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A previous study showed that several multivalent galactose-specific lectins including the 14-kDa lectin from calf spleen and the lectins from Erythrina indica, Erythrina cristagalli, and soybean agglutinin formed specific cross-linked complexes with the glycoprotein asialofetuin (ASF) [Mandal, D.
Redefinition of the carbohydrate specificity of Erythrina corallodendron lectin based on solid-phase binding assays and molecular modeling of native and recombinant forms obtained by site-directed mutagenesis.
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Binding of the N-acetyllactosamine-specific lectin from Erythrina corallodendron (ECorL) to four glycosphingolipids has been tested using the microtiter well assay. The role of several amino acids in the binding site region was studied by combining binding assays and molecular modeling for native
Effect of glycosylation on the structure of Erythrina corallodendron lectin.
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The three-dimensional structure of the recombinant form of Erythrina corallodendron lectin, complexed with lactose, has been elucidated by X-ray crystallography at 2.55 A resolution. Comparison of this non-glycosylated structure with that of the native glycosylated lectin reveals that the tertiary
Expression of Erythrina corallodendron lectin in Escherichia coli.
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The cDNA of the Erythrina corallodendron lectin (ECorL) has been expressed in Escherichia coli. For this purpose, an NcoI site was inserted into the cDNA coding for the lectin precursor [Arango, R., Rozenblatt, S. & Sharon, N. (1990) FEBS Lett. 264, 109-112] immediately before the codon GTG
Mutational studies of the amino acid residues in the combining site of Erythrina corallodendron lectin.
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High-resolution X-ray crystallography of the complex of the Gal/GalNAc-specific Erythrina corallodendron lectin with lactose identified the amino acid side chains that form contacts with the galactose moiety of the disaccharide. The contribution of these amino acids to the binding of different
Modification of the sugar specificity of a plant lectin: structural studies on a point mutant of Erythrina corallodendron lectin.
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A mutant of Erythrina corallodendron lectin was generated with the aim of enhancing its affinity for N-acetylgalactosamine. A tyrosine residue close to the binding site of the lectin was mutated to a glycine in order to facilitate stronger interactions between the acetamido group of the sugar and
Expression of Gal beta 1-4GlcNAc sequences by human gastrointestinal neoplasms and their precursors as detected by Erythrina cristagalli and Erythrina corallodendron lectins.
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Lectins from Erythrina cristagalli (EGA) and Erythrina corallodendron (ECorA) are well-known to detect type 2 chain oligosaccharides (Gal beta 1-4GlcNAc). These carbohydrate moieties are the biosynthetic precursors of various ABH and Lewis blood group antigens and are therefore also related to
Common architecture of the primary galactose binding sites of Erythrina corallodendron lectin and heat-labile enterotoxin from Escherichia coli in relation to the binding of branched neolactohexaosylceramide.
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The heat-labile enterotoxin from Escherichia coli (LT) is responsible for so-called traveller's diarrhea and is closely related to the cholera toxin (CT). Toxin binding to GM1 at the epithelial cell surface of the small intestine initiates the subsequent diarrheal disease. However, LT has a broader
Carbohydrate specificity and salt-bridge mediated conformational change in acidic winged bean agglutinin.
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Structures of two crystal forms of the dimeric acidic winged bean agglutinin (WBAII) complexed with methyl-alpha-D-galactose have been determined at 3.0 A and 3.3 A resolution. The subunit structure and dimerisation of the lectin are similar to those of the basic lectin from winged bean (WBAI) and
Carbohydrate specificity and quaternary association in basic winged bean lectin: X-ray analysis of the lectin at 2.5 A resolution.
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The structure of basic Winged Bean Agglutinin (WBAI) with two dimeric molecules complexed with methyl-alpha-D-galactopyranoside in the asymmetric unit, has been determined by the molecular replacement method and refined with 2.5 A X-ray intensity data. The polypeptide chain of each monomer has the
Molecular dynamics simulations of oligosaccharides and their conformation in the crystal structure of lectin-carbohydrate complex: importance of the torsion angle psi for the orientation of alpha 1,6-arm.
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The conformation of the heptasaccharide Man-alpha 1,6-(Man-alpha 1,3)(Xyl-beta 1,2)-Man-beta 1,4-GlcNAc2-beta 1,4-(L- Fuc-alpha 1,3)-GlcNAc1, the carbohydrate moiety of Erythrina corallodendron lectin (EcorL), the hexasaccharide Man-alpha 1,6-(Man-alpha 1,3) (GlcNAc-beta 1,4)-Man-beta
How proteins bind carbohydrates: lessons from legume lectins.
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The pioneering studies of Irvin Liener on soybean agglutinin (SBA) in the early 1950s served as the starting point of our involvement in lectin research during the past four decades. Initially we characterized SBA extensively as a glycoprotein and showed that its covalently linked glycan is an
Role of N-linked glycan in the unfolding pathway of Erythrina corallodendron lectin.
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Identifikohuni Regjistrohu
Erythrina corallodendron lectin (ECorL) exhibits an exquisitely structured oligosaccharide chain. Interestingly, the bacterially expressed, nonglycosylated counterpart, rECorL, possesses an essentially identical carbohydrate specificity and agglutinating activity as the glycosylated lectin, thus
The primary structure of the acidic lectin from winged bean (Psophocarpus tetragonolobus): insights in carbohydrate recognition, adenine binding and quaternary association.
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The amino acid sequence of the winged bean acidic lectin (WBA II) was determined by chemical means and by recombinant techniques. From the N- and C-terminal sequence, obtained chemically, primers were designed for PCR amplification of the genomic DNA. The PCR product was cloned and sequenced to get
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