Structure-function analysis of protein active sites with anti-idiotypic antibody.
Antigen and internal image-bearing anti-idiotypic antibody, owing to potential differences in size and chemical nature, need not necessarily demonstrate identical binding specificities. Such differences, termed "dissociability," may be exploited in structure-function analysis of receptor-ligand interaction to identify functionally important amino acid residues, define receptor class, or distinguish receptor conformation. In this sense, ligand and the anti-idiotypes they elicit constitute alternative and complementary probes of protein active sites.
Ludwig
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Schoolnik
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D000595:Amino Acid Sequence; D000888:Antibodies, Anti-Idiotypic; D000911:Antibodies, Monoclonal; D000918:Antibody Specificity; D000936:Antigen-Antibody Complex / Q000032:analysis; D001665:Binding Sites; D002678:Chimera; D002772:Cholera Toxin / Q000276:immunology; D008024:Ligands; D008961:Models, Structural; D008969:Molecular Sequence Data; D011485:Protein Binding; D011506:Proteins / Q000032:analysis* / Q000276:immunology
D000888:Antibodies, Anti-Idiotypic; D000911:Antibodies, Monoclonal; D000936:Antigen-Antibody Complex; D008024:Ligands; D011506:Proteins; D002772:Cholera Toxin