2N81

Solution Structure of Lipid Transfer Protein From Pea Pisum Sativum

2N81 の概要

• エントリーDOI: 10.2210/pdb2n81/pdb
• NMR情報: BMRB: 25830
• 分子名称: Lipid Transfer Protein (1 entity in total)
• 機能のキーワード: lipid binding, antimicrobial activity, allergen, lipid binding protein, antimicrobial protein
• 由来する生物種: Pisum sativum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9546.00

構造登録者

Paramonov, A.S.,Rumynskiy, E.I.,Bogdanov, I.V.,Finkina, E.I.,Melnikova, D.N.,Ovchinnikova, T.V.,Shenkarev, Z.O.,Arseniev, A.S. (登録日: 2015-09-30, 公開日: 2016-05-11, 最終更新日: 2024-11-20)

主引用文献

Bogdanov, I.V.,Shenkarev, Z.O.,Finkina, E.I.,Melnikova, D.N.,Rumynskiy, E.I.,Arseniev, A.S.,Ovchinnikova, T.V.
A novel lipid transfer protein from the pea Pisum sativum: isolation, recombinant expression, solution structure, antifungal activity, lipid binding, and allergenic properties.
BMC Plant Biol, 16:107-107,

PubMed Abstract: Plant lipid transfer proteins (LTPs) assemble a family of small (7-9 kDa) ubiquitous cationic proteins with an ability to bind and transport lipids as well as participate in various physiological processes including defense against phytopathogens. They also form one of the most clinically relevant classes of plant allergens. Nothing is known to date about correlation between lipid-binding and IgE-binding properties of LTPs. The garden pea Pisum sativum is widely consumed crop and important allergenic specie of the legume family. This work is aimed at isolation of a novel LTP from pea seeds and characterization of its structural, functional, and allergenic properties.

PubMed: 27137920
DOI: 10.1186/s12870-016-0792-6

実験手法

SOLUTION NMR