2N81

Solution Structure of Lipid Transfer Protein From Pea Pisum Sativum

Summary for 2N81

• Entry DOI: 10.2210/pdb2n81/pdb
• NMR Information: BMRB: 25830
• Descriptor: Lipid Transfer Protein (1 entity in total)
• Functional Keywords: lipid binding, antimicrobial activity, allergen, lipid binding protein, antimicrobial protein
• Biological source: Pisum sativum
• Total number of polymer chains: 1
• Total formula weight: 9546.00

Authors

Paramonov, A.S.,Rumynskiy, E.I.,Bogdanov, I.V.,Finkina, E.I.,Melnikova, D.N.,Ovchinnikova, T.V.,Shenkarev, Z.O.,Arseniev, A.S. (deposition date: 2015-09-30, release date: 2016-05-11, Last modification date: 2024-11-20)

Primary citation

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

Experimental method

SOLUTION NMR