4WFU
Bovine allergen Bos d 2 in the trigonal space group P3221.
Summary for 4WFU
| Entry DOI | 10.2210/pdb4wfu/pdb |
| Related | 1BJ7 |
| Descriptor | Allergen Bos d 2 (2 entities in total) |
| Functional Keywords | allergen, lipocalin |
| Biological source | Bos taurus (Bovine) |
| Cellular location | Secreted: Q28133 |
| Total number of polymer chains | 1 |
| Total formula weight | 17867.98 |
| Authors | Niemi, M.H.,Rouvinen, J. (deposition date: 2014-09-17, release date: 2015-09-16, Last modification date: 2024-10-16) |
| Primary citation | Niemi, M.H.,Rytkonen-Nissinen, M.,Miettinen, I.,Janis, J.,Virtanen, T.,Rouvinen, J. Dimerization of lipocalin allergens. Sci Rep, 5:13841-13841, 2015 Cited by PubMed Abstract: Lipocalins are one of the most important groups of inhalant animal allergens. The analysis of structural features of these proteins is important to get insights into their allergenicity. We have determined two different dimeric crystal structures for bovine dander lipocalin Bos d 2, which was earlier described as a monomeric allergen. The crystal structure analysis of all other determined lipocalin allergens also revealed oligomeric structures which broadly utilize inherent structural features of the β-sheet in dimer formation. According to the moderate size of monomer-monomer interfaces, most of these dimers would be transient in solution. Native mass spectrometry was employed to characterize quantitatively transient dimerization of two lipocalin allergens, Bos d 2 and Bos d 5, in solution. PubMed: 26346541DOI: 10.1038/srep13841 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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