title: Remarkable remote chiral recognition in a reaction mediated by a catalytic antibody.
abstract: The crystal structures of catalytic antibody D2.3 Fab with the two enantiomers, 7D and 7L, which represent transition state analogues for the hydrolysis of the corresponding esters, 6D and 6L, were determined to better understand remarkable reactivity differences: the L-ester displayed significantly tighter binding (K(M)) and increased catalytic activity (k(cat)) with D2.3, even though the chiral center is 7 bonds distant from the reaction center. Surprisingly, the electron densities of the liganded phosphonates, 7D and 7L, within the D2.3 binding/reaction site were essentially identical, highlighting the subtle influences of protein interactions on chemical behavior.
authors.affiliation: Department of Pharmaceutical Chemistry, The Hebrew University, School of Pharmacy, P.O. Box 12065, Jerusalem 91120, Israel.
authors.forename: Lawrence J
authors.initials: LJ
authors.lastname: D'Souza
authors.forename: Benoît
authors.initials: B
authors.lastname: Gigant
authors.forename: Marcel
authors.initials: M
authors.lastname: Knossow
authors.forename: Bernard S
authors.initials: BS
authors.lastname: Green
mesh_terms: D017151:Antibodies, Catalytic / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D006241:Haptens / Q000737:chemistry; D006868:Hydrolysis; D007700:Kinetics; D063065:Organophosphonates / Q000737:chemistry; D011487:Protein Conformation; D013237:Stereoisomerism
chemical_list: D017151:Antibodies, Catalytic; D006241:Haptens; D063065:Organophosphonates