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 Cited by PubMed: 26559323DOI: 10.1016/j.jaci.2015.09.026 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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