1qh2 | pdb_00001qh2
CHYMOTRYPSIN INHIBITOR (C2) FROM NICOTIANA ALATA
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| 1qh2 | |||||||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Overview
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.
About this Structure
1QH2 is a Protein complex structure of sequences from Nicotiana alata. Full crystallographic information is available from OCA.
Reference
A novel two-chain proteinase inhibitor generated by circularization of a multidomain precursor protein., Lee MC, Scanlon MJ, Craik DJ, Anderson MA, Nat Struct Biol. 1999 Jun;6(6):526-30. PMID:10360353
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