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.

@article{Valjakka2002CrystalSO,
  title={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.},
  author={Jarkko Valjakka and Ari Hemminki and Seija Niemi and Hans S{\"o}derlund and Kristiina Takkinen and Juha Rouvinen},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 46},
  pages={44021-7}
}
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 mutations and has about 40-fold increased affinity (K(d) = 3 x 10(-10) m) when compared… CONTINUE READING