Canonical binding arrays as molecular recognition elements in the immune system: tetrahedral anions and the ester hydrolysis transition state.
The structures, obtained by X-ray crystallography, of the binding sites of catalytic antibodies raised to bind different phosphonates are compared. Although the amino acid sequences differ, all exhibit a tetrahedral array of hydrogen bond donors (a 'canonical binding array') complementary to the tetrahedral anion, which represents a 'transition state epitope' for the basic hydrolysis of esters and amides. Antibodies for phosphates, arsonates, and sulfonates are found also to possess the tetrahedral anion canonical binding array.
Tantillo
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DJ
Department of Chemistry and Biochemistry, University of California, Los Angeles, 405 Hilgard Avenue, 90095-1569, Los Angeles, CA, USA.
Houk
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KN
D000818:Animals; D000838:Anions; D000906:Antibodies / Q000737:chemistry* / Q000276:immunology / Q000378:metabolism*; D000918:Antibody Specificity; D018360:Crystallography, X-Ray; D000939:Epitopes / Q000737:chemistry* / Q000378:metabolism; D004952:Esters; D006241:Haptens / Q000276:immunology* / Q000378:metabolism; D006801:Humans; D006868:Hydrolysis; D011487:Protein Conformation
D000838:Anions; D000906:Antibodies; D000939:Epitopes; D004952:Esters; D006241:Haptens