Article
Crystal structure of an in vitro affinity- and specificity-matured anti-testosterone Fab in complex with testosterone. Improved affinity results from small structural changes within the variable domains.
The Journal of biological chemistry - 15 Nov 2002
Valjakka Jarkko, Hemminki Ari, Niemi Seija, Söderlund Hans, Takkinen Kristiina, Rouvinen Juha
Abstract excerpt
A highly selective, high affinity recombinant anti-testosterone Fab fragment has been generated by stepwise optimization of the complementarity-determining regions (CDRs) by random mutagenesis and phage display selection of a monoclonal antibody (3-C(4)F(5)). The best mutant (77 Fab) was obtained by evaluating the additivity effects of different independently selected CDR mutations. The 77 Fab contains 20...
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