2vxq | pdb_00002vxq

CRYSTAL STRUCTURE OF THE MAJOR GRASS POLLEN ALLERGEN PHL P 2 IN COMPLEX WITH ITS SPECIFIC IGE-FAB

spinqualitylabelsall models 2vxq, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2vxq is a 3 chain structure with sequence from Common timothy and Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1bmw, 1whp, 1who Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed We report the three-dimensional structure of the complex between the major respiratory grass pollen allergen Phl p 2 and its specific human IgE-derived Fab. The Phl p 2-specific human IgE Fab has been isolated from a combinatorial library constructed from lymphocytes of a pollen allergic patient. When the variable domains of the IgE Fab were grafted onto human IgG1, the resulting Ab (huMab2) inhibited strongly the binding of allergic patients' IgE to Phl p 2 as well as allergen-induced basophil degranulation. Analysis of the binding of the allergen to the Ab by surface plasmon resonance yielded a very low dissociation constant (K(D) = 1.1 x 10(-10) M), which is similar to that between IgE and Fcepsilon;RI. The structure of the Phl p 2/IgE Fab complex was determined by x-ray crystallography to 1.9 A resolution revealing a conformational epitope (876 A(2)) comprised of the planar surface of the four-stranded anti-parallel beta-sheet of Phl p 2. The IgE-defined dominant epitope is discontinuous and formed by 21 residues located mostly within the beta strands. Of the 21 residues, 9 interact directly with 5 of the 6 CDRs (L1, L3, H1, H2, H3) of the IgE Fab predominantly by hydrogen bonding and van der Waals interactions. Our results indicate that IgE Abs recognize conformational epitopes with high affinity and provide a structural basis for the highly efficient effector cell activation by allergen/IgE immune complexes. High-affinity IgE recognition of a conformational epitope of the major respiratory allergen Phl p 2 as revealed by X-ray crystallography.,Padavattan S, Flicker S, Schirmer T, Madritsch C, Randow S, Reese G, Vieths S, Lupinek C, Ebner C, Valenta R, Markovic-Housley Z J Immunol. 2009 Feb 15;182(4):2141-51. PMID:19201867 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Antibody

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