• Corpus ID: 20884276

Crystal structure of delta-chymotrypsin bound to a peptidyl chloromethyl ketone inhibitor.

@article{MacSweeney2000CrystalSO,
  title={Crystal structure of delta-chymotrypsin bound to a peptidyl chloromethyl ketone inhibitor.},
  author={Aengus Mac Sweeney and Gabriel Birrane and Martin A. Walsh and T P O'connell and J. Paul G. Malthouse and Tim Higgins},
  journal={Acta crystallographica. Section D, Biological crystallography},
  year={2000},
  volume={56 Pt 3},
  pages={
          280-6
        }
}
Chymotrypsin is a member of the trypsin family of serine proteases and is one of the first proteins successfully studied by X-ray crystallography. It is secreted into the intestine as the inactive precursor chymotrypsinogen; four sequential cleavages of the peptide bonds following residues 13, 15, 146 and 148 occur to generate the active pi, delta, kappa and alpha forms of chymotrypsin. (13)C NMR has shown [O'Connell & Malthouse (1995). Biochem. J. 307, 353-359] that when the delta form of… 

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