4BK7: Crystal Structure Of A Variant Of The Major Birch Pollen Allergen Bet V 1

Citation:
Abstract
Many allergens share several biophysical characteristics, including the capability to undergo oligomerization. The dimerization mechanism in Bet v 1 and its allergenic properties are so far poorly understood. Here, we report crystal structures of dimeric Bet v 1, revealing a noncanonical incorporation of cysteine at position 5 instead of genetically encoded tyrosine. Cysteine polysulfide bridging stabilized different dimeric assemblies, depending on the polysulfide linker length. These dimers represent quaternary arrangements that are frequently observed in related proteins, reflecting their prevalence in unmodified Bet v 1. These conclusions were corroborated by characteristic immunologic properties of monomeric and dimeric allergen variants. Hereby, residue 5 could be identified as an allergenic hot spot in Bet v 1. The presented results refine fundamental principles in protein chemistry and emphasize the importance of protein modifications in understanding the molecular basis of allergenicity.
PDB ID: 4BK7Download
MMDB ID: 115398
PDB Deposition Date: 2013/4/22
Updated in MMDB: 2013/11
Experimental Method:
x-ray diffraction
Resolution: 1.14  Å
Source Organism:
Similar Structures:
Biological Unit for 4BK7: monomeric; determined by author and by software (PISA)
Molecular Components in 4BK7
Label Count Molecule
Protein (1 molecule)
1
Major Pollen Allergen BET V 1-A
Molecule annotation
Chemicals (9 molecules)
1
5
2
3
3
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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