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 89 residues consists of two hevein-like domains with the same spacing or 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.
