2N81

Solution Structure of Lipid Transfer Protein From Pea Pisum Sativum


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 300 
  • Conformers Submitted: 20 
  • Selection Criteria: target function 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

A novel lipid transfer protein from the pea Pisum sativum: isolation, recombinant expression, solution structure, antifungal activity, lipid binding, and allergenic properties.

Bogdanov, I.V.Shenkarev, Z.O.Finkina, E.I.Melnikova, D.N.Rumynskiy, E.I.Arseniev, A.S.Ovchinnikova, T.V.

(null) Bmc Plant Biol 16: 107-107

  • DOI: https://doi.org/10.1186/s12870-016-0792-6
  • Primary Citation of Related Structures:  
    2N81

  • 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.


  • Organizational Affiliation

    M.M.Shemyakin and Yu.A.Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya str., 16/10, 117997, Moscow, Russia.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Lipid Transfer Protein95Pisum sativumMutation(s): 0 
UniProt
Find proteins for A0A161AT60 (Pisum sativum)
Explore A0A161AT60 
Go to UniProtKB:  A0A161AT60
Find proteins for A0A182DV18 (Pisum sativum)
Explore A0A182DV18 
Go to UniProtKB:  A0A182DV18
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupsA0A161AT60A0A182DV18
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 300 
  • Conformers Submitted: 20 
  • Selection Criteria: target function 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2016-05-11
    Type: Initial release
  • Version 1.1: 2017-12-20
    Changes: Database references