title: The amino acid sequence of peanut agglutinin.
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 concanavalin 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.
authors.affiliation: Institute for Biological Sciences, National Research Council of Canada, Ottawa, Ontario.
authors.forename: N M
authors.initials: NM
authors.lastname: Young
authors.forename: R A
authors.initials: RA
authors.lastname: Johnston
authors.forename: D C
authors.initials: DC
authors.lastname: Watson
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D050260:Carbohydrate Metabolism; D037102:Lectins / Q000737:chemistry*; D008969:Molecular Sequence Data; D019887:Peanut Agglutinin
chemical_list: D037102:Lectins; D019887:Peanut Agglutinin