Structural evidence for a programmed general base in the active site of a catalytic antibody.

ABSTRACT: The crystal structure of the complex of a catalytic antibody with its cationic hapten at 1.9-A resolution demonstrates that the hapten amidinium group is stabilized through an ionic pair interaction with the carboxylate of a combining-site residue. The location of this carboxylate allows it to act as a general base in an allylic rearrangement. When compared with structures of other antibody complexes in which the positive moiety of the hapten is stabilized mostly by cation-pi interactions, this structure shows that the amidinium moiety is a useful candidate to elicit a carboxylate in an antibody combining site at a predetermined location with respect to the hapten. More generally, this structure highlights the advantage of a bidentate hapten for the programmed positioning of a chemically r

SUBMITTER: Golinelli-Pimpaneau B 

PROVIDER: S-EPMC27617 | biostudies-literature | 2000 Aug

REPOSITORIES: biostudies-literature