4a84

Crystal Structure of Major Birch Pollen Allergen Bet v 1 a F30V mutant in complex with deoxycholate.

spinqualitylabelsall models 4a84, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4a84 is a 1 chain structure with sequence from Betpn. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: DXC, MPD, SO4 Related: 1llt, 1fsk, 1qmr, 1b6f, 4a80, 1btv, 1bv1, 4a81, 4a83 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [BEV1A_BETPN] May be a general steroid carrier protein (By similarity). Publication Abstract from PubMed 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 A. 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. Crystallographically Mapped Ligand Binding Differs in High and Low IgE Binding Isoforms of Birch Pollen Allergen Bet v 1.,Kofler S, Asam C, Eckhard U, Wallner M, Ferreira F, Brandstetter H J Mol Biol. 2012 Sep 7;422(1):109-23. Epub 2012 May 23. PMID:22634284 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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