The primary structure of stinging nettle (Urtica dioica) agglutinin. A two-domain member of the hevein family.
The primary structure of stinging nettle (Urtica dioica) agglutinin has been determined by sequence analysis of peptides obtained from three overlapping proteolytic digests. The sequence of 80 residues consists of two hevein-like domains with the same spacing of half-cystine residues and several other conserved residues as observed earlier in other proteins with hevein-like domains. The hinge region between the two domains is four residues longer than those between the four domains in cereal lectins like wheat germ agglutinin.
Beintema
J J
JJ
Biochemisch Laboratorium, Groningen, The Netherlands.
Peumans
W J
WJ
D000373:Agglutinins / Q000235:genetics*; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D023181:Antimicrobial Cationic Peptides; D002851:Chromatography, High Pressure Liquid; D008969:Molecular Sequence Data; D037121:Plant Lectins; D010940:Plant Proteins / Q000235:genetics*; D010947:Plants, Toxic / Q000378:metabolism*; D016415:Sequence Alignment
D000373:Agglutinins; D000596:Amino Acids; D023181:Antimicrobial Cationic Peptides; D037121:Plant Lectins; D010940:Plant Proteins; C045875:hevein