2MAR

Solution structure of Ani s 5 Anisakis simplex allergen


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • 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

Relationships between IgE/IgG4 epitopes, structure and function in Anisakis simplex Ani s 5, a member of the SXP/RAL-2 protein family

Garcia-Mayoral, M.F.Trevino, M.A.Perez-Pinar, T.Caballero, M.L.Knaute, T.Umpierrez, A.Bruix, M.Rodriguez-Perez, R.

(2014) PLoS Negl Trop Dis 8: e2735-e2735

  • DOI: https://doi.org/10.1371/journal.pntd.0002735
  • Primary Citation of Related Structures:  
    2MAR

  • PubMed Abstract: 

    Anisakiasis is a re-emerging global disease caused by consumption of raw or lightly cooked fish contaminated with L3 Anisakis larvae. This zoonotic disease is characterized by severe gastrointestinal and/or allergic symptoms which may misdiagnosed as appendicitis, gastric ulcer or other food allergies. The Anisakis allergen Ani s 5 is a protein belonging to the SXP/RAL-2 family; it is detected exclusively in nematodes. Previous studies showed that SXP/RAL-2 proteins are active antigens; however, their structure and function remain unknown. The aim of this study was to elucidate the three-dimensional structure of Ani s 5 and its main IgE and IgG4 binding regions.


  • Organizational Affiliation

    Institute of Physical Chemistry "Rocasolano". CSIC. Madrid, Spain.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
SXP/RAL-2 family protein134Anisakis simplexMutation(s): 0 
Gene Names: Ani s 5
UniProt
Find proteins for A1IKL2 (Anisakis simplex)
Explore A1IKL2 
Go to UniProtKB:  A1IKL2
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA1IKL2
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • 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: 2014-07-02
    Type: Initial release
  • Version 1.1: 2023-06-14
    Changes: Data collection, Database references, Other