Conversion of trypsin to a functional threonine protease

@article{Baird2006ConversionOT,
  title={Conversion of trypsin to a functional threonine protease},
  author={Teaster T. Baird and W. Wright and C. Craik},
  journal={Protein Science},
  year={2006},
  volume={15}
}
The hydroxyl group of a serine residue at position 195 acts as a nucleophile in the catalytic mechanism of the serine proteases. However, the chemically similar residue, threonine, is rarely used in similar functional context. Our structural modeling suggests that the Ser 195 → Thr trypsin variant is inactive due to negative steric interaction between the methyl group on the β‐carbon of Thr 195 and the disulfide bridge formed by cysteines 42 and 58. By simultaneously truncating residues 42 and… Expand
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