1VB8

solution structure of vhr1, the first cyclotide from root tissue

1VB8 の概要

• エントリーDOI: 10.2210/pdb1vb8/pdb
• 分子名称: Viola hederacea root peptide 1 (1 entity in total)
• 機能のキーワード: cyclotide, cystine knot, circular, viola, cck, plant protein
• 由来する生物種: Viola hederacea
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3136.71

構造登録者

Trabi, M.,Craik, D.J. (登録日: 2004-02-25, 公開日: 2004-12-21, 最終更新日: 2024-10-23)

主引用文献

Trabi, M.,Craik, D.J.
Tissue-specific expression of head-to-tail cyclized miniproteins in Violaceae and structure determination of the root cyclotide Viola hederacea root cyclotide1
Plant Cell, 16:2204-2216, 2004

PubMed Abstract: The plant cyclotides are a family of 28 to 37 amino acid miniproteins characterized by their head-to-tail cyclized peptide backbone and six absolutely conserved Cys residues arranged in a cystine knot motif: two disulfide bonds and the connecting backbone segments form a loop that is penetrated by the third disulfide bond. This knotted disulfide arrangement, together with the cyclic peptide backbone, renders the cyclotides extremely stable against enzymatic digest as well as thermal degradation, making them interesting targets for both pharmaceutical and agrochemical applications. We have examined the expression patterns of these fascinating peptides in various Viola species (Violaceae). All tissue types examined contained complex mixtures of cyclotides, with individual profiles differing significantly. We provide evidence for at least 57 novel cyclotides present in a single Viola species (Viola hederacea). Furthermore, we have isolated one cyclotide expressed only in underground parts of V. hederacea and characterized its primary and three-dimensional structure. We propose that cyclotides constitute a new family of plant defense peptides, which might constitute an even larger and, in their biological function, more diverse family than the well-known plant defensins.

PubMed: 15295104
DOI: 10.1105/tpc.104.021790

実験手法

SOLUTION NMR