1o0v | pdb_00001o0v

The crystal structure of IgE Fc reveals an asymmetrically bent conformation

spinqualitylabelsall models 1o0v, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1o0v is a 2 chain structure with sequence from Homo sapiens. This structure supersedes the now removed PDB entry 1ls0. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BMA, GOL, SO4, MAN, NAG Gene: IgE(ND) (Homo sapiens) Resources: FirstGlance, OCA, 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 The distinguishing structural feature of immunoglobulin E (IgE), the antibody responsible for allergic hypersensitivity, is the C epsilon 2 domain pair that replaces the hinge region of IgG. The crystal structure of the IgE Fc (constant fragment) at a 2.6-A resolution has revealed these domains. They display a distinctive, disulfide-linked Ig domain interface and are folded back asymmetrically onto the C epsilon 3 and C epsilon 4 domains, which causes an acute bend in the IgE molecule. The structure implies that a substantial conformational change involving C epsilon 2 must accompany binding to the mast cell receptor Fc epsilon RI. This may be the basis of the exceptionally slow dissociation rate of the IgE-Fc epsilon RI complex and, thus, of the ability of IgE to cause persistent allergic sensitization of mast cells. The crystal structure of IgE Fc reveals an asymmetrically bent conformation.,Wan T, Beavil RL, Fabiane SM, Beavil AJ, Sohi MK, Keown M, Young RJ, Henry AJ, Owens RJ, Gould HJ, Sutton BJ Nat Immunol. 2002 Jul;3(7):681-6. Epub 2002 Jun 17. PMID:12068291 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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