HIGH RESOLUTION (>2 0 E) CRYSTAL STRUCTURE OF CATALYTIC ANTIBODIES

Stanford University, Stanford CA

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Abstract

Structural studies of catalytic antibodies in my laboratory focuses on six systems (i) Antibody-catalyzed ester hydrolysis, (ii) An antibody ferrochelastase, (iii) Antibody-catalyzed aminoacylation reaction, (iv) An antibody-catalyzed regio- and stereoselective ketone reduction. To date, the field of catalytic antibodies has suffered from not having high resolution crystal structures to aid in the hapten/transition state ligand design. Without improved hapten design, the field will have a difficult time in improving the catalytic rates of the abzymes and in achieving the catalytic rates that are comparable to enzymes. Thus it is critical to obtain the highest resolution data possible to carefully understand how the catalytic antibodies function.