Primary structure of the Dolichos biflorus seed lectin

The Dolichos biflorus seed lectin is a tetramer composed of equal amounts of two subunit types. The subunit types are structurally very similar, yet only the larger subunit exhibits the ability to bind carbohydrate. A cDNA clone representing the entire coding region of the D. biflorus lectin mRNA ha...

Full description

Saved in:
Bibliographic Details
Published in:The Journal of biological chemistry 1987-05, Vol.262 (15), p.7220-7225
Main Authors: Schnell, D J, Etzler, M E
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Base Sequence
Binding Sites
Biological and medical sciences
carbohidratos
Carbohydrate Metabolism
carbohydrates
Concanavalin A
DNA
DNA - genetics
DNA, Recombinant
Dolichos biflorus
Fabaceae
Fundamental and applied biological sciences. Psychology
genes
glucide
graine
lablab purpureus
lectina
lectine
lectins
Lectins - genetics
Metals - metabolism
Miscellaneous
nucleotide sequence
peptide
Peptide Fragments - genetics
peptides
peptidos
Plant Lectins
Plants, Medicinal
proteinas
proteine
Proteins
RNA, Messenger - genetics
seeds
semilla
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The Dolichos biflorus seed lectin is a tetramer composed of equal amounts of two subunit types. The subunit types are structurally very similar, yet only the larger subunit exhibits the ability to bind carbohydrate. A cDNA clone representing the entire coding region of the D. biflorus lectin mRNA has been sequenced. This cDNA represents 1075 nucleotides of seed lectin mRNA encoding a polypeptide of Mr = 29,674. Analysis of the deduced sequence indicates that the NH2 termini and COOH termini of both lectin subunits are present within the mRNA coding region. This information supports previous data indicating that both subunits of the lectin are encoded by a single mRNA and that the difference between the subunit types apparently arises by the proteolytic removal of a 10-amino acid sequence from the COOH terminus of the larger subunit. Comparison of the D. biflorus seed lectin sequence to the sequence of other leguminous seed lectins indicates regions of extensive homology. The residues of concanavalin A involved in metal binding are highly conserved in the D. biflorus lectin, but those involved in saccharide binding show a much lower degree of conservation. Prediction of the secondary conformation of the D. biflorus polypeptide suggests that structures involved in the formation of quaternary structure in concanavalin A are also conserved.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)48226-9