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 tet...

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Veröffentlicht in:Chemistry & Biology 2001-06, Vol.8 (6), p.535-545
Hauptverfasser: Tantillo, Dean J, Houk, K.N
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description 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.
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subjects Animals
Anions
Antibodies - chemistry
Antibodies - immunology
Antibodies - metabolism
Antibody Specificity
Canonical binding array
Crystallography, X-Ray
Epitopes - chemistry
Epitopes - metabolism
Esters
Haptens - immunology
Haptens - metabolism
Humans
Hydrolysis
Immune system
Molecular recognition
Protein Conformation
Tetrahedral anion
title Canonical binding arrays as molecular recognition elements in the immune system: tetrahedral anions and the ester hydrolysis transition state
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