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Title: A novel two-chain proteinase inhibitor generated by circularization of a multidomain precursor protein. Author: Lee MC, Scanlon MJ, Craik DJ, Anderson MA. Journal: Nat Struct Biol; 1999 Jun; 6(6):526-30. PubMed ID: 10360353. Abstract: Female reproductive tissues of the ornamental tobacco amass high levels of serine proteinase inhibitors (PIs) for protection against pests and pathogens. These PIs are produced from a precursor protein composed of six repeats each with a protease reactive site. Here we show that proteolytic processing of the precursor generates five single-chain PIs and a remarkable two-chain inhibitor formed by disulfide-bond linkage of N- and C-terminal peptide fragments. Surprisingly, PI precursors adopt this circular structure regardless of the number of inhibitor domains, suggesting this bracelet-like conformation is characteristic of the widespread potato inhibitor II (Pot II) protein family.[Abstract] [Full Text] [Related] [New Search]