Novel reactions catalysed by antibodies.
New structural data on nonhydrolytic antibody catalysts gained over the past two years confirm that antibodies elicited against transition-state analogues function by differential stabilisation of the transition-state over the ground state through electrostatic, van der Waals, cation-pi and hydrogen-bonding interactions. The lack of chemical catalysis correlates with the low catalytic efficiency. Novel strategies that precisely position a key functional residue in the antibody catalyst combining site have therefore emerged, as demonstrated by crystallographic studies. Whereas antibodies with a bulky residue at position H100c of hypervariable loop H3 adopt different cavity shapes, other antibodies share a common deep combining site. This structural restriction might reflect the use of similar hydrophobic haptens to generate the antibody; novel hapten design or new immunisation strategies may, in the future, lead to more structurally diversified active sites.
Golinelli-Pimpaneau
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Laboratoire d'Enzymologie et Biochimie Structurales, CNRS Bât 34, 1 avenue de la Terrasse, 91198 Cedex, Gif-sur-Yvette, France. beatrice.golinelli@lebs.cnrs-gif.fr
D017151:Antibodies, Catalytic / Q000737:chemistry / Q000378:metabolism*; D002384:Catalysis; D008190:Lyases / Q000378:metabolism; D008958:Models, Molecular; D011487:Protein Conformation
D017151:Antibodies, Catalytic; D008190:Lyases