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The primary structure of stinging nettle ( Urtica dioica ) agglutinin A two‐domain member of the hevein family
Author(s) -
Beintema Jaap J.,
Peumans Willy J.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80231-5
Subject(s) - urtica dioica , agglutinin , wheat germ agglutinin , sequence (biology) , protein primary structure , biology , biochemistry , peptide sequence , botany , lectin , gene
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.