7KYW
Crystal structure of timothy grass allergen Phl p 12.0101 reveals an unusual profilin dimer
Summary for 7KYW
| Entry DOI | 10.2210/pdb7kyw/pdb |
| Descriptor | Profilin-1, CITRIC ACID (3 entities in total) |
| Functional Keywords | grass allergy, allergen, profilin, phleum pratense, pollen-food syndrome, oral allergy syndrome |
| Biological source | Phleum pratense (Common timothy) |
| Total number of polymer chains | 1 |
| Total formula weight | 14368.30 |
| Authors | O'Malley, A.,Kapingidza, A.B.,Hyduke, N.,Dolamore, C.,Chruszcz, M. (deposition date: 2020-12-09, release date: 2021-03-31, Last modification date: 2024-11-06) |
| Primary citation | O'Malley, A.,Kapingidza, A.B.,Hyduke, N.,Dolamore, C.,Kowal, K.,Chruszcz, M. Crystal structure of timothy grass allergen Phl p 12.0101 reveals an unusual profilin dimer. Acta Biochim.Pol., 68:15-22, 2021 Cited by PubMed Abstract: Timothy grass pollen is a source of potent allergens. Among them, Phl p 1 and Phl p 5 are thought to be the most important, as a majority of timothy grass-allergic individuals have IgE antibodies directed against these two allergens. The profilin from timothy grass (Phl p 12) has been registered as a minor allergen, with up to 35% of individuals in populations of grass pollen allergic patients showing IgE binding to Phl p 12. Profilins are primarily minor allergens and are known for a high likelihood of co-sensitization as well as cross-reactivity situations caused by their sequence and structure similarity. The crystal structure of Phl p 12.0101 was determined and it revealed that this allergen may form an unusual dimer not previously observed among any profilins. For example, the Phl p 12 dimer has a completely different geometry and interface when compared with the latex profilin (Hev b 8) dimer that has its crystal structure determined. The structure of Phl p 12.0101 is described in the context of allergenic sensitization and allergy diagnostics. Moreover, the structure of the Phl p 12.0101 dimer is discussed, taking into account the production of recombinant allergens and their storage. PubMed: 33720678DOI: 10.18388/abp.2020_5587 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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