4qip | pdb_00004qip

Crystal Structure of Major Birch Pollen Allergen Bet v 1 isoform a in complex with Sodium Dodecyl Sulfate

spinqualitylabelsall models 4qip, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4qip 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 2Å Ligands: SDS, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BEV1A_BETPN May be a general steroid carrier protein (By similarity). Publication Abstract from PubMed Pathogenesis-related plant proteins of class-10 (PR-10) are essential for storage and transport of small molecules. A prominent member of the PR-10 family, the major birch pollen allergen Bet v 1, is the main cause of spring pollinosis in the temperate climate zone of the northern hemisphere. Bet v 1 binds various ligand molecules to its internal cavity, and immunologic effects of the presence of ligand have been discussed. However, the mechanism of binding has remained elusive. In this study, we show that in solution Bet v 1.0101 is conformationally heterogeneous and cannot be represented by a single structure. NMR relaxation data suggest that structural dynamics are fundamental for ligand access to the protein interior. Complex formation then leads to significant rigidification of the protein along with a compaction of its 3D structure. The data presented herein provide a structural basis for understanding the immunogenic and allergenic potential of ligand binding to Bet v 1 allergens. Ligand binding modulates the structural dynamics and compactness of the major birch pollen allergen.,Grutsch S, Fuchs JE, Freier R, Kofler S, Bibi M, Asam C, Wallner M, Ferreira F, Brandstetter H, Liedl KR, Tollinger M Biophys J. 2014 Dec 16;107(12):2963-72. doi: 10.1016/j.bpj.2014.10.062. PMID:25517162 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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