Studies on phytohemagglutinins. XXVII. A study of the pea lectin binding site.
Under defined mild conditions the reaction of the pea lectin with 2-nitrophenylsulfenyl chloride results in sulfenylation of only 2 of the 10 tryptophan residues of the lectin molecule with simultaneous loss of biological activity. Both sulfenylated tryptophan residues belong to the two heavy subunits of the lectin. Enzymic hydrolysis and separation of the tryptic peptides yields only one homogeneous yellow peptide containing the modified tryptophan residue. The isolated peptide has the following sequence (NPS, nitrophenylsulfenyl): HAsp-Val-Val-Pro-Glu-(2-NPS-Trp)-Val-ArgOH. The octapeptide is either directly a part of the pea lectin binding site or it plays an important role in maintaining the tertiary structure of the binding site. According to the amino acid composition and amino acid sequence, the octapeptide isolated from the pea lectin is almost identical with that part of the peptide chain of concanavalin A near to which the location of the sugar binding site is supposed to be.
D000595:Amino Acid Sequence; D001665:Binding Sites; D002118:Calcium / Q000032:analysis; D003208:Concanavalin A; D037102:Lectins; D008345:Manganese / Q000032:analysis; D008958:Models, Molecular; D009578:Nitrobenzenes; D009842:Oligopeptides; D011487:Protein Conformation; D013434:Sulfenic Acids; D014357:Trypsin
D037102:Lectins; D009578:Nitrobenzenes; D009842:Oligopeptides; D013434:Sulfenic Acids; D003208:Concanavalin A; D008345:Manganese; D014357:Trypsin; D002118:Calcium