Changes in structure and dynamics of the Fv fragment of a catalytic antibody upon binding of inhibitor.

ABSTRACT: Binding of the product inhibitor p-nitrophenol to the monoclonal esterolytic antibody NPN43C9 has been investigated by performing NMR spectroscopy of the heterodimeric variable-domain fragment (Fv) of the antibody in the presence and absence of inhibitor. Structural information from changes in chemical shift upon binding has been related to the changes in local dynamics in the active site of the catalytic antibody using NMR relaxation measurements. Significant changes in the chemical shifts of the backbone resonances upon binding extend beyond the immediate vicinity of the antigen binding site into the interface between the two associated polypeptides that form the Fv heterodimer, a possible indication that the binding of ligand causes a change in the relative orientations of the component

SUBMITTER: Kroon GJ 

PROVIDER: S-EPMC2323930 | biostudies-literature | 2003 Jul

REPOSITORIES: biostudies-literature