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Potato lectin: an updated model of a unique chimeric plant protein
Author(s) -
Van Damme Els J. M.,
Barre Annick,
Rougé Pierre,
Peumans Willy J.
Publication year - 2004
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1046/j.1365-313x.2003.01929.x
Subject(s) - biology , lectin , solanaceae , complementary dna , peptide sequence , c type lectin , chimera (genetics) , recombinant dna , amino acid , tandem repeat , biochemistry , genetics , computational biology , gene , genome
Summary A complete cDNA encoding a potato tuber lectin has been identified and sequenced. Based on the deduced amino acid sequence, the still enigmatic molecular structure of the classical chimeric potato lectin could eventually be determined. Basically, the potato lectin consists of two nearly identical chitin‐binding modules, built up of two in‐tandem arrayed hevein domains that are interconnected by an extensin‐like domain of approximately 60 amino acid residues. Although this structure confirms the ‘canonical’ chimeric nature of the Solanaceae lectins, it differs fundamentally from all previously proposed models. The new insights in the structure are also discussed in view of the physiological role of the Solanaceae lectins.