6FRR

Structural and immunological properties of the allergen Art v 3


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.95 Å
  • R-Value Free: 0.249 
  • R-Value Work: 0.193 
  • R-Value Observed: 0.196 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Boiling down the cysteine-stabilized LTP fold - loss of structural and immunological integrity of allergenic Art v 3 and Pru p 3 as a consequence of irreversible lanthionine formation.

Wildner, S.Griessner, I.Stemeseder, T.Regl, C.Soh, W.T.Stock, L.G.Volker, T.Alessandri, C.Mari, A.Huber, C.G.Stutz, H.Brandstetter, H.Gadermaier, G.

(2019) Mol Immunol 116: 140-150

  • DOI: https://doi.org/10.1016/j.molimm.2019.10.012
  • Primary Citation of Related Structures:  
    6FRR

  • PubMed Abstract: 

    Non-specific lipid transfer proteins (LTPs) are important allergens in fruits, pollen, vegetables, nuts and latex. Due to their compact structure, LTPs are highly resistant to heat treatment. Here, Art v 3 from mugwort pollen and Pru p 3 from peach were used as model allergens to in-depth investigate structural and immunological properties upon thermal treatment at different buffer conditions.


  • Organizational Affiliation

    Department of Biosciences, University of Salzburg, Salzburg, Austria; Christian Doppler Laboratory for Innovative Tools for the Characterization of Biosimilars, University of Salzburg, Salzburg, Austria.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Non-specific lipid-transfer protein
A, B
92Artemisia vulgarisMutation(s): 0 
Gene Names: Art v 3
UniProt
Find proteins for C4MGG9 (Artemisia vulgaris)
Explore C4MGG9 
Go to UniProtKB:  C4MGG9
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupC4MGG9
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.95 Å
  • R-Value Free: 0.249 
  • R-Value Work: 0.193 
  • R-Value Observed: 0.196 
  • Space Group: P 32 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 60.398α = 90
b = 60.398β = 90
c = 91.46γ = 120
Software Package:
Software NamePurpose
PHENIXrefinement
MOSFLMdata reduction
SCALAdata scaling
REFMACphasing
Cootmodel building

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Austrian Science FundAustriaW_1213

Revision History  (Full details and data files)

  • Version 1.0: 2019-03-13
    Type: Initial release
  • Version 1.1: 2020-03-25
    Changes: Database references
  • Version 1.2: 2024-01-17
    Changes: Advisory, Data collection, Database references, Refinement description