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PDBsum entry 5jt8

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protein ligands metals Protein-protein interface(s) links
Allergen PDB id
5jt8

 

 

 

 

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Contents
Protein chains
310 a.a.
Ligands
NAG-NAG
NAG
NO3 ×6
Metals
_CL ×4
Waters ×306
PDB id:
5jt8
Name: Allergen
Title: Structural basis for the limited antibody cross reactivity between the mite allergens blo t 1 and der p 1
Structure: Blo t 1 allergen. Chain: a, b. Engineered: yes
Source: Blomia tropicalis. Mite. Organism_taxid: 40697. Expressed in: komagataella pastoris. Expression_system_taxid: 4922
Resolution:
2.10Å     R-factor:   0.173     R-free:   0.217
Authors: K.Meno,J.S.Kastrup,M.Gajhede
Key ref: K.H.Meno et al. (2017). The structure of the mite allergen Blo t 1 explains the limited antibody cross-reactivity to Der p 1. Allergy, 72, 665-670. PubMed id: 27997997 DOI: 10.1111/all.13111
Date:
09-May-16     Release date:   24-May-17    
PROCHECK
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 Headers
 References

Protein chains
A1KXI0  (CYSP_BLOTA) -  Cysteine protease from Blomia tropicalis
Seq:
Struc:
333 a.a.
310 a.a.*
Key:    Secondary structure
* PDB and UniProt seqs differ at 6 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.3.4.22.-  - ?????
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1111/all.13111 Allergy 72:665-670 (2017)
PubMed id: 27997997  
 
 
The structure of the mite allergen Blo t 1 explains the limited antibody cross-reactivity to Der p 1.
K.H.Meno, J.S.Kastrup, I.C.Kuo, K.Y.Chua, M.Gajhede.
 
  ABSTRACT  
 
The Blomia tropicalis (Blo t) mite species is considered a storage mite in temperate climate zones and an important source of indoor allergens causing allergic asthma and rhinitis in tropical and subtropical regions. Here, we report the crystal structure of one of the allergens from Blo t, recombinant proBlo t 1 (rproBlo t 1), determined at 2.1 Å resolution. Overall, the fold of rproBlo t 1 is characteristic for the pro-form of cysteine proteases from the C1A class. Structural comparison of experimentally mapped Der f 1/Der p1 IgG epitopes to the same surface patch on Blo t 1, as well as of sequence identity of surface-exposed residues, suggests limited cross-reactivity between these allergens and Blo t 1. This is in agreement with ELISA inhibition results showing that, although cross-reactive human IgE epitopes exist, there are unique IgE epitopes for both Blo t 1 and Der p 1.
 

 

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