4A83
Crystal Structure of Major Birch Pollen Allergen Bet v 1 a in complex with deoxycholate.
Summary for 4A83
| Entry DOI | 10.2210/pdb4a83/pdb |
| Related | 1B6F 1BTV 1BV1 1FSK 1LLT 1QMR 4A80 4A81 4A84 4A85 4A86 4A87 4A88 4A8G |
| Descriptor | MAJOR POLLEN ALLERGEN BET V 1-A, (3ALPHA,5BETA,12ALPHA)-3,12-DIHYDROXYCHOLAN-24-OIC ACID, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | allergen, pr-10 protein |
| Biological source | BETULA PENDULA (EUROPEAN WHITE BIRCH) |
| Cellular location | Cytoplasm: P15494 |
| Total number of polymer chains | 1 |
| Total formula weight | 18845.23 |
| Authors | Kofler, S.,Brandstetter, H. (deposition date: 2011-11-18, release date: 2012-05-30, Last modification date: 2023-12-20) |
| Primary citation | Kofler, S.,Asam, C.,Eckhard, U.,Wallner, M.,Ferreira, F.,Brandstetter, H. Crystallographically Mapped Ligand Binding Differs in High and Low Ige Binding Isoforms of Birch Pollen Allergen Bet V 1. J.Mol.Biol., 422:109-, 2012 Cited by PubMed Abstract: The ability of pathogenesis-related proteins of family 10 to bind a broad spectrum of ligands is considered to play a key role for their physiological and pathological functions. In particular, Bet v 1, an archetypical allergen from birch pollen, is described as a highly promiscuous ligand acceptor. However, the detailed recognition mechanisms, including specificity factors discriminating binding properties of naturally occurring Bet v 1 variants, are poorly understood. Here, we report crystal structures of Bet v 1 variants in complex with an array of ligands at a resolution of up to 1.2 Å. Residue 30 within the hydrophobic pocket not only discriminates in high and low IgE binding Bet v 1 isoforms but also induces a drastic change in the binding mode of the model ligand deoxycholate. Ternary crystal structure complexes of Bet v 1 with several ligands together with the fluorogenic reporter 1-anilino-8-naphthalene sulfonate explain anomalous fluorescence binding curves obtained from 1-anilino-8-naphthalene sulfonate displacement assays. The structures reveal key interaction residues such as Tyr83 and rationalize both the binding specificity and promiscuity of the so-called hydrophobic pocket in Bet v 1. The intermolecular interactions of Bet v 1 reveal an unexpected complexity that will be indispensable to fully understand its roles within the physiological and allergenic context. PubMed: 22634284DOI: 10.1016/J.JMB.2012.05.016 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.54 Å) |
Structure validation
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