2KPY

Solution Structure of the major allergen of Artemisia vulgaris (Art v 1)


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with the lowest energy 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Mapping the interactions between a major pollen allergen and human IgE antibodies.

Razzera, G.Gadermaier, G.de Paula, V.Almeida, M.S.Egger, M.Jahn-Schmid, B.Almeida, F.C.Ferreira, F.Valente, A.P.

(2010) Structure 18: 1011-1021

  • DOI: https://doi.org/10.1016/j.str.2010.05.012
  • Primary Citation of Related Structures:  
    2KPY

  • PubMed Abstract: 

    The interaction of specific IgE antibodies with allergens is a key event in the induction of allergic symptoms, thus representing an important target for therapeutic interventions in Type I allergies. We report here the solution NMR structure of Art v 1, the major mugwort pollen allergen. Art v 1 is the first protein structure with an allergenic defensin fold linked to a polyproline domain, which has not been identified in any reported allergen structure in the PDB. Moreover, the direct interaction of polyclonal IgE antibodies from an allergic patient has been mapped on the surface of an allergen for the first time. The data presented herein provide the basis for the design of tools for safe and effective vaccination against mugwort pollen allergy.


  • Organizational Affiliation

    Centro Nacional de Ressonância Magnética Nuclear, Universidade Federal do Rio de Janeiro, Instituto de Bioquímica Médica, Rio de Janeiro, Brazil.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Major pollen allergen Art v 1108Artemisia vulgarisMutation(s): 0 
UniProt
Find proteins for Q84ZX5 (Artemisia vulgaris)
Explore Q84ZX5 
Go to UniProtKB:  Q84ZX5
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ84ZX5
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with the lowest energy 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-10-06
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2020-02-26
    Changes: Data collection, Database references, Other
  • Version 1.3: 2023-06-14
    Changes: Database references, Other