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The binding site on human immunoglobulin E for its high affinity receptor. 1994

L Presta, and R Shields, and L O'Connell, and S Lahr, and J Porter, and C Gorman, and P Jardieu
Department of Protein Engineering, Genentech Inc., South San Francisco, California 94080.

Immunoglobulin (Ig) E antibodies mediate allergic responses by binding to specific high affinity receptors, Fc epsilon RI, on mast cells and basophils. Previous studies have shown that the principal Fc epsilon RI binding site is located on the third constant domain, Fc epsilon 3, of IgE. Based on a model of the IgE Fc epsilon 3 (which is homologous to the second constant domain of IgG), homology scanning mutagenesis and replacement of individual residues were used to determine the specific amino acids of human IgE involved in binding to human Fc epsilon RI. The amino acids are localized in three loops, which form a putative ridge on the most exposed side of the Fc epsilon 3 domain of IgE and include Arg-408, Ser-411, Lys-415, Glu-452, Arg-465, and Met-469. The preponderance of charged residues suggests that IgE-Fc epsilon RI binding is mediated primarily by electrostatic interaction. Furthermore, it is possible to confer Fc epsilon RI binding to an IgG molecule by introducing these three IgE loops into the IgG C gamma 2 domain.

UI MeSH Term Description Entries
D007073 Immunoglobulin E An immunoglobulin associated with MAST CELLS. Overexpression has been associated with allergic hypersensitivity (HYPERSENSITIVITY, IMMEDIATE). IgE
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D001665 Binding Sites The parts of a macromolecule that directly participate in its specific combination with another molecule. Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D013329 Structure-Activity Relationship The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups. Relationship, Structure-Activity,Relationships, Structure-Activity,Structure Activity Relationship,Structure-Activity Relationships
D017455 Receptors, IgE Specific molecular sites on the surface of B- and T-lymphocytes which combine with IgEs. Two subclasses exist: low affinity receptors (Fc epsilon RII) and high affinity receptors (Fc epsilon RI). Antigens, CD23,CD23 Antigens,Fc Receptors, epsilon,Fc epsilon Receptor,Fc epsilon Receptors,IgE Receptor,IgE Receptors,Receptors, Fc epsilon,epsilon Fc Receptor,epsilon Fc Receptors,CD 23 Antigens,CD23 Antigen,Fc epsilon RI,Fc epsilon RII,Immunoglobulin E Receptor,Antigen, CD23,Antigens, CD 23,Fc Receptor, epsilon,Receptor, Fc epsilon,Receptor, IgE,Receptor, Immunoglobulin E,Receptor, epsilon Fc,Receptors, epsilon Fc,epsilon RI, Fc,epsilon RII, Fc,epsilon Receptor, Fc,epsilon Receptors, Fc

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