The amino acid sequence of peanut agglutinin
Open Access
- 3 March 1991
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 196 (3), 631-637
- https://doi.org/10.1111/j.1432-1033.1991.tb15859.x
Abstract
The amino acid sequence of peanut (Arachis hypogaea) agglutinin was determined from three major fragments obtained by mild acid cleavage at Asp-Pro peptide bonds. The sequence of 236 amino acids has residues identical to those that form the metal-binding site and the hydrophobic pocket in concanavlin A and other lectins, although the overall similarity is only 42%. In the segments of peanut agglutinin that correspond to the four loops that form the carbohydrate-binding site in concanavalin A and favin, several central residues are homologous, while others show changes to smaller side chains, such as Tyr → Gly. The carbohydrate-binding site of peanut agglutinin may therefore have a similar peptide-backbone architecture, but form a considerably more open cleft.Keywords
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