2LJS

Solution structure of MCoTI-V

2LJS の概要

• エントリーDOI: 10.2210/pdb2ljs/pdb
• 関連するPDBエントリー: 1nb1
• NMR情報: BMRB: 17956
• 分子名称: Trypsin inhibitor 3 (1 entity in total)
• 機能のキーワード: beta strand, helix, cyclic backbone, hydrolase inhibitor
• 由来する生物種: Momordica cochinchinensis (Spiny bitter cucumber)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3320.92

構造登録者

Daly, N.L.,Craik, D.J. (登録日: 2011-09-23, 公開日: 2012-08-08, 最終更新日: 2024-10-30)

主引用文献

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

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: 22822203
DOI: 10.1105/tpc.112.099085

実験手法

SOLUTION NMR