6NRE
Monomeric Lipocalin Can F 6
Summary for 6NRE
| Entry DOI | 10.2210/pdb6nre/pdb |
| Descriptor | Lipocalin-Can f 6 allergen (2 entities in total) |
| Functional Keywords | lipocalin, metabolic role, allergen |
| Biological source | Canis lupus familiaris (Dog) |
| Total number of polymer chains | 1 |
| Total formula weight | 21046.69 |
| Authors | Clayton G, M.,Kappler J, W.,Chan, S. (deposition date: 2019-01-23, release date: 2019-09-25, Last modification date: 2024-11-06) |
| Primary citation | Clayton, G.M.,White, J.,Lee, S.,Kappler, J.W.,Chan, S.K. Structural characteristics of lipocalin allergens: Crystal structure of the immunogenic dog allergen Can f 6. Plos One, 14:e0213052-e0213052, 2019 Cited by PubMed Abstract: Lipocalins represent the most important protein family of the mammalian respiratory allergens. Four of the seven named dog allergens are lipocalins: Can f 1, Can f 2, Can f 4, and Can f 6. We present the structure of Can f 6 along with data on the biophysical and biological activity of this protein in comparison with other animal lipocalins. The Can f 6 structure displays the classic lipocalin calyx-shaped ligand binding cavity within a central β-barrel similar to other lipocalins. Despite low sequence identity between the different dog lipocalin proteins, there is a high degree of structural similarity. On the other hand, Can f 6 has a similar primary sequence to cat, horse, mouse lipocalins as well as a structure that may underlie their cross reactivity. Interestingly, the entrance to the ligand binding pocket is capped by a His instead of the usually seen Tyr that may help select its natural ligand binding partner. Our highly pure recombinant Can f 6 is able to bind to human IgE (hIgE) demonstrating biological antigenicity. PubMed: 31525203DOI: 10.1371/journal.pone.0213052 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.06 Å) |
Structure validation
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