2GL1
NMR solution structure of Vigna radiata Defensin 2 (VrD2)
2GL1 の概要
エントリーDOI | 10.2210/pdb2gl1/pdb |
NMR情報 | BMRB: 7092 |
分子名称 | PDF1 (1 entity in total) |
機能のキーワード | antimicrobial, plant defensin, cysteine-stabilized alfa/beta motif, plant protein |
由来する生物種 | Vigna radiata |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 5514.21 |
構造登録者 | Lin, K.F.,Lee, T.R.,Tsai, P.H.,Hsu, M.P.,Chen, C.S.,Lyu, P.C. (登録日: 2006-04-04, 公開日: 2007-04-03, 最終更新日: 2024-11-13) |
主引用文献 | Lin, K.F.,Lee, T.R.,Tsai, P.H.,Hsu, M.P.,Chen, C.S.,Lyu, P.C. Structure-based protein engineering for alpha-amylase inhibitory activity of plant defensin. Proteins, 68:530-540, 2007 Cited by PubMed Abstract: The structure of a novel plant defensin isolated from the seeds of the mung bean, Vigna radiate, has been determined by (1)H nuclear magnetic resonance spectroscopy. The three-dimensional structure of VrD2, the V. radiate plant defensin 2 protein, comprises an alpha-helix and one triple-stranded anti-parallel beta-sheet stabilized by four disulfide bonds. This protein exhibits neither insecticidal activity nor alpha-amylase inhibitory activity in spite of showing a similar global fold to that of VrD1, an insecticidal plant defensin that has been suggested to function by inhibiting insect alpha-amylase. Our previous study proposed that loop L3 of plant defensins is important for this inhibition. Structural analyses and surface charge comparisons of VrD1 and VrD2 revealed that the charged residues of L3 correlate with the observed difference in inhibitory activities of these proteins. A VrD2 chimera that was produced by transferring the proposed functional loop of VrD1 onto the structurally equivalent loop of VrD2 supported this hypothesis. The VrD2 chimera, which differs by only five residues compared with VrD2, showed obvious activity against Tenebrio molitor alpha-amylase. These results clarify the mode of alpha-amylase inhibition of plant defensins and also represent a possible approach for engineering novel alpha-amylase inhibitors. Plant defensins are important constituents of the innate immune system of plants, and thus the application of protein engineering to this protein family may provide an efficient method for protecting against crop losses. PubMed: 17444520DOI: 10.1002/prot.21378 主引用文献が同じPDBエントリー |
実験手法 | SOLUTION NMR |
構造検証レポート
検証レポート(詳細版)
をダウンロード
