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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1993-1-25
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pubmed:abstractText |
Twelve plant lectins from the Papilionoideae subfamily were selected to represent a range of carbohydrate specificities, and their sequences were aligned. Two variability indices were applied to the aligned sequences and the results were analysed using the three-dimensional structures of concanavalin A and the pea lectin. The areas of greatest variability were located in the carbohydrate-binding site region, forming a perimeter around a well-conserved core. These residues are inferred to be specificity determining, in the manner of antibodies, and the most variable position corresponded to Tyr100 in concanavalin A, a known ligand contact residue. In addition to the five peptide loops known to form the binding site from crystallographic studies, a sixth segment with variable residues was located in the binding-site region, and this may contribute to oligosaccharide specificity. In their overall composition, the lectin sites resemble those of the sugar-transport proteins rather than antibodies. The prospects for modelling lectin binding sites by the methods used for antibodies were also assessed.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0022-2836
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
228
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
924-34
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:1469724-Amino Acid Sequence,
pubmed-meshheading:1469724-Binding Sites,
pubmed-meshheading:1469724-Carbohydrate Metabolism,
pubmed-meshheading:1469724-Concanavalin A,
pubmed-meshheading:1469724-Fabaceae,
pubmed-meshheading:1469724-Genetic Variation,
pubmed-meshheading:1469724-Lectins,
pubmed-meshheading:1469724-Models, Molecular,
pubmed-meshheading:1469724-Molecular Sequence Data,
pubmed-meshheading:1469724-Plant Lectins,
pubmed-meshheading:1469724-Plants, Medicinal,
pubmed-meshheading:1469724-Sequence Alignment,
pubmed-meshheading:1469724-Sequence Analysis,
pubmed-meshheading:1469724-Sequence Homology, Amino Acid,
pubmed-meshheading:1469724-Structure-Activity Relationship
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pubmed:year |
1992
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pubmed:articleTitle |
Analysis of sequence variation among legume lectins. A ring of hypervariable residues forms the perimeter of the carbohydrate-binding site.
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pubmed:affiliation |
Institute for Biological Sciences, National Research Council of Canada, Ottawa, Ontario, Canada.
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pubmed:publicationType |
Journal Article,
Comparative Study
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