2LB7

Hevein-type Antifungal Peptide with a Unique 10-Cysteine Motif

2LB7 の概要

• エントリーDOI: 10.2210/pdb2lb7/pdb
• NMR情報: BMRB: 17547
• 分子名称: Antimicrobial peptide 1a (1 entity in total)
• 機能のキーワード: antimicrobial protein
• 由来する生物種: Triticum kiharae (Wheat)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4450.06

構造登録者

Balashova, T.A.,Vassilevski, A.A.,Odintsova, T.I.,Grishin, E.V.,Egorov, T.A.,Arseniev, A.S. (登録日: 2011-03-23, 公開日: 2011-04-13, 最終更新日: 2024-11-20)

主引用文献

Dubovskii, P.V.,Vassilevski, A.A.,Slavokhotova, A.A.,Odintsova, T.I.,Grishin, E.V.,Egorov, T.A.,Arseniev, A.S.
Solution structure of a defense peptide from wheat with a 10-cysteine motif.
Biochem.Biophys.Res.Commun., 411:14-18, 2011

PubMed Abstract: Hevein, a well-studied lectin from the rubber tree Hevea brasiliensis, is the title representative of a broad family of chitin-binding polypeptides. WAMP-1a, a peptide isolated from the wheat Triticum kiharae, shares considerable similarity with hevein. The peptide possesses antifungal, antibacterial activity and is thought to play an important role in the defense system of wheat. Importantly, it features a substitution of the conserved serine residue to glycine reducing its carbohydrate-binding capacity. We used NMR spectroscopy to derive the spatial structure of WAMP-1a in aqueous solution. Notably, the mutation was found to strengthen amphiphilicity of the molecule, associated with its mode of action, an indication of the hevein domain multi-functionality. Both primary and tertiary structure of WAMP-1a suggest its evolutionary origin from the hevein domain of plant chitinases.

PubMed: 21704019
DOI: 10.1016/j.bbrc.2011.06.058

実験手法

SOLUTION NMR