4bk7

Crystal Structure of a variant of the Major Birch Pollen Allergen Bet v 1

spinqualitylabelsall models 4bk7, resolution 1.14Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4bk7 is a 1 chain structure with sequence from Betula pendula. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.14Å Ligands: MPD, NA, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BEV1A_BETPN May be a general steroid carrier protein (By similarity). Publication Abstract from PubMed Many allergens share several biophysical characteristics, including the capability to undergo oligomerisation. The dimerization mechanism in Bet v 1 and its allergenic properties are so far poorly understood. Here, we report crystal structures of dimeric Bet v 1, revealing a non-canonical incorporation of cysteine at position 5 instead of genetically encoded tyrosine. Cysteine polysulfide bridging stabilized different dimeric assemblies, depending on the polysulfide linker length. These dimers represent quaternary arrangements that are frequently observed in related proteins, reflecting their prevalence in unmodified Bet v 1. These conclusions were corroborated by characteristic immunologic properties of monomeric and dimeric allergen variants. Hereby, residue 5 could be identified as an allergenic hot spot in Bet v 1. The presented results refine fundamental principles in protein chemistry, and emphasize the importance of protein modifications in understanding the molecular basis of allergenicity. Stabilization of the dimeric birch pollen allergen Bet v 1 impacts its immunological properties.,Kofler S, Ackaert C, Samonig M, Asam C, Briza P, Horejs-Hoeck J, Cabrele C, Ferreira F, Duschl A, Huber C, Brandstetter H J Biol Chem. 2013 Nov 19. PMID:24253036 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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