Conservation and variability in the structures of serine proteinases of the chymotrypsin family.

@article{Lesk1996ConservationAV,
  title={Conservation and variability in the structures of serine proteinases of the chymotrypsin family.},
  author={Arthur M. Lesk and W D Fordham},
  journal={Journal of molecular biology},
  year={1996},
  volume={258 3},
  pages={501-37}
}
The chymotrypsin-like serine proteinases are a widely divergent family of enzymes appearing in animals, bacteria and viruses. All comprise two homologous domains containing six-stranded beta-barrels, with the active site between the domains. What are the structural constraints to which these proteins have been subject during their evolution, and how have the molecules explored the limits these constraints impose? We have analysed the structures of 13 widely divergent serine proteinases… CONTINUE READING