1QH2
CHYMOTRYPSIN INHIBITOR (C2) FROM NICOTIANA ALATA
Summary for 1QH2
| Entry DOI | 10.2210/pdb1qh2/pdb |
| Descriptor | PROTEIN (TRYPSIN INHIBITOR C2) (2 entities in total) |
| Functional Keywords | proteinase inhibitor (chymotrypsin), serine proteinase inhibitor, potato ii trypsin inhibitor, nicotiana alata, hydrolase inhibitor |
| Biological source | Nicotiana alata (Persian tobacco) More |
| Total number of polymer chains | 2 |
| Total formula weight | 5023.82 |
| Authors | Lee, M.C.S.,Scanlon, M.J.,Anderson, M.A.,Craik, D.J. (deposition date: 1999-05-11, release date: 1999-05-24, Last modification date: 2024-11-13) |
| Primary citation | Lee, M.C.,Scanlon, M.J.,Craik, D.J.,Anderson, M.A. A novel two-chain proteinase inhibitor generated by circularization of a multidomain precursor protein. Nat.Struct.Biol., 6:526-530, 1999 Cited by PubMed 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. PubMed: 10360353DOI: 10.1038/9293 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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