4Z3L

CRYSTAL STRUCTURE OF BIRCH POLLEN ALLERGEN BET V 1 MUTANT G26L, D69I, P90L, K97I

Summary for 4Z3L

• Entry DOI: 10.2210/pdb4z3l/pdb
• Descriptor: Major pollen allergen Bet v 1-A, SULFATE ION (3 entities in total)
• Functional Keywords: allergen, fold stability
• Biological source: Betula pendula (European white birch)
• Cellular location: Cytoplasm: P15494
• Total number of polymer chains: 6
• Total formula weight: 106439.62

Authors

Freier, R.,Brandstetter, H. (deposition date: 2015-03-31, release date: 2015-11-25, Last modification date: 2024-01-10)

Primary citation

Machado, Y.,Freier, R.,Scheiblhofer, S.,Thalhamer, T.,Mayr, M.,Briza, P.,Grutsch, S.,Ahammer, L.,Fuchs, J.E.,Wallnoefer, H.G.,Isakovic, A.,Kohlbauer, V.,Hinterholzer, A.,Steiner, M.,Danzer, M.,Horejs-Hoeck, J.,Ferreira, F.,Liedl, K.R.,Tollinger, M.,Lackner, P.,Johnson, C.M.,Brandstetter, H.,Thalhamer, J.,Weiss, R.
Fold stability during endolysosomal acidification is a key factor for allergenicity and immunogenicity of the major birch pollen allergen.
J.Allergy Clin.Immunol., 137:1525-1534, 2016

PubMed Abstract: The search for intrinsic factors, which account for a protein's capability to act as an allergen, is ongoing. Fold stability has been identified as a molecular feature that affects processing and presentation, thereby influencing an antigen's immunologic properties.

PubMed: 26559323
DOI: 10.1016/j.jaci.2015.09.026

Experimental method

X-RAY DIFFRACTION (2.5 Å)