2M64

1H, 13C and 15N Chemical Shift Assignments for Phl p 5a


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 10 
  • Selection Criteria: structures with the lowest energy 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Flexible IgE epitope-containing domains of Phl p 5 cause high allergenic activity.

Gobl, C.Focke-Tejkl, M.Najafi, N.Schrank, E.Madl, T.Kosol, S.Madritsch, C.Dorofeeva, Y.Flicker, S.Thalhamer, J.Valenta, R.Zangger, K.Tjandra, N.

(2017) J Allergy Clin Immunol 140: 1187-1191

  • DOI: https://doi.org/10.1016/j.jaci.2017.05.005
  • Primary Citation of Related Structures:  
    2M64

  • PubMed Abstract: 

    This is the first study determining the three-dimensional structure of Phl p 5a which reveals a novel mechanism for high allergenic activity based on flexibly connected IgE-reactive domains which cross-link effector cell-bound IgE more efficiently than isolated rigid globular proteins. These findings may also form a basis for specific immunotherapy strategies.


  • Organizational Affiliation

    Institute of Chemistry/Organic and Bioorganic Chemistry, University of Graz, Graz, Austria; Institute of Structural Biology, Helmholtz Zentrum München, Neuherberg, Germany; Biomolecular NMR, Department of Chemistry, Technische Universität München, Garching, Germany; Laboratory of Molecular Biophysics, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Md.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Phlp5231Phleum pratenseMutation(s): 0 
UniProt
Find proteins for Q40960 (Phleum pratense)
Explore Q40960 
Go to UniProtKB:  Q40960
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ40960
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 10 
  • 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: 2014-03-26
    Type: Initial release
  • Version 1.1: 2018-02-28
    Changes: Database references
  • Version 1.2: 2023-06-14
    Changes: Data collection, Database references, Other