title: Characterization of residues in human IgE and IgG binding site by chemical modification of ovomucoid third domain.
abstract: Chemical modification of ovomucoid third domain (DIII) has been conducted to characterize the binding site residues that determine antigenecity and allergenecity of DIII. Nitration of Tyr, ethoxyformylation of His and succinylation of Lys residues led to a decrease of alpha-helix content of DIII. Modification of His, Tyr, Glu, Asp and Lys residues on DIII resulted in a reduction of human IgG binding activity, but little effect on IgE binding activity. These results suggest that hydrophilic residues appear to be more critical for human IgG binding site, whereas hydrophobic residues may be more important for IgG binding site.
authors.affiliation: Department of Food Science, University of Guelph, Guelph, Ontario, N1G 2W1, Canada.
authors.forename: J W
authors.initials: JW
authors.lastname: Zhang
authors.forename: Y
authors.initials: Y
authors.lastname: Mine
mesh_terms: D000215:Acylation; D000478:Alkylation; D001224:Aspartic Acid / Q000737:chemistry; D001665:Binding Sites; D002675:Child, Preschool; D002942:Circular Dichroism; D005260:Female; D018698:Glutamic Acid / Q000737:chemistry; D006639:Histidine / Q000737:chemistry; D006801:Humans; D007073:Immunoglobulin E / Q000737:chemistry* / Q000378:metabolism; D007074:Immunoglobulin G / Q000737:chemistry* / Q000378:metabolism; D007223:Infant; D008239:Lysine / Q000737:chemistry; D010059:Ovomucin / Q000737:chemistry* / Q000378:metabolism; D017433:Protein Structure, Secondary; D013329:Structure-Activity Relationship; D013774:Tetranitromethane / Q000737:chemistry; D014443:Tyrosine / Q000737:chemistry
chemical_list: D007074:Immunoglobulin G; D001224:Aspartic Acid; D010059:Ovomucin; D007073:Immunoglobulin E; D018698:Glutamic Acid; D014443:Tyrosine; D006639:Histidine; D013774:Tetranitromethane; D008239:Lysine