|Title||Inhibition of ligand exchange kinetics via active-site trapping with an antibody fragment.|
|Publication Type||Journal Article|
|Year of Publication||2014|
|Authors||Oyen, D., Steyaert J., and Barlow J. N.|
|Date Published||2014 Apr 01|
|Keywords||Catalytic Domain, Crystallography, X-Ray, Escherichia coli, Kinetics, Ligands, Protein Structure, Secondary, Single-Domain Antibodies, Tetrahydrofolate Dehydrogenase|
We describe the first example of an inhibitory antibody fragment (nanobody ca1697) that binds simultaneously to an enzyme (the enzyme dihydrofolate reductase from Escherichia coli) and its bound substrate (folate). Binding of the antibody to the substrate causes a 20-fold reduction in the rate of folate exchange kinetics. This work opens up the prospect of designing new types of antibody-based inhibitors of enzymes and receptors through suitable design of immunogens.
Inhibition of ligand exchange kinetics via active-site trapping with an antibody fragment.