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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.

Abstract Title:

Potato lectin: an updated model of a unique chimeric plant protein.

Abstract Source:

Plant J. 2004 Jan;37(1):34-45. PMID: 14675430

Abstract Author(s):

Els J M Van Damme, Annick Barre, Pierre Rougé, Willy J Peumans

Article Affiliation:

Department of Molecular Biotechnology, Ghent University, Coupure Links 653, 9000 Gent, Belgium. ElsJM.Van Damme@UGent.be

Abstract:

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.


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Study Type : In Vitro Study
Additional Links
Problem Substances : Potato Lectin : CK(4) : AC(4)

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