2LJS
Solution structure of MCoTI-V
Summary for 2LJS
| Entry DOI | 10.2210/pdb2ljs/pdb |
| Related | 1nb1 |
| NMR Information | BMRB: 17956 |
| Descriptor | Trypsin inhibitor 3 (1 entity in total) |
| Functional Keywords | beta strand, helix, cyclic backbone, hydrolase inhibitor |
| Biological source | Momordica cochinchinensis (Spiny bitter cucumber) |
| Total number of polymer chains | 1 |
| Total formula weight | 3320.92 |
| Authors | Daly, N.L.,Craik, D.J. (deposition date: 2011-09-23, release date: 2012-08-08, Last modification date: 2024-10-30) |
| Primary citation | Mylne, J.S.,Chan, L.Y.,Chanson, A.H.,Daly, N.L.,Schaefer, H.,Bailey, T.L.,Nguyencong, P.,Cascales, L.,Craik, D.J. Cyclic Peptides Arising by Evolutionary Parallelism via Asparaginyl-Endopeptidase-Mediated Biosynthesis. Plant Cell, 24:2765-2778, 2012 Cited by PubMed Abstract: The cyclic miniprotein Momordica cochinchinensis Trypsin Inhibitor II (MCoTI-II) (34 amino acids) is a potent trypsin inhibitor (TI) and a favored scaffold for drug design. We have cloned the corresponding genes and determined that each precursor protein contains a tandem series of cyclic TIs terminating with the more commonly known, and potentially ancestral, acyclic TI. Expression of the precursor protein in Arabidopsis thaliana showed that production of the cyclic TIs, but not the terminal acyclic TI, depends on asparaginyl endopeptidase (AEP) for maturation. The nature of their repetitive sequences and the almost identical structures of emerging TIs suggest these cyclic peptides evolved by internal gene amplification associated with recruitment of AEP for processing between domain repeats. This is the third example of similar AEP-mediated processing of a class of cyclic peptides from unrelated precursor proteins in phylogenetically distant plant families. This suggests that production of cyclic peptides in angiosperms has evolved in parallel using AEP as a constraining evolutionary channel. We believe this is evolutionary evidence that, in addition to its known roles in proteolysis, AEP is especially suited to performing protein cyclization. PubMed: 22822203DOI: 10.1105/tpc.112.099085 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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