The Crystal and Molecular Structure of DIP-inhibited Bovine Trypsin at 2.7Å Resolution
This extract was created in the absence of an abstract.
Excerpt
Mammalian pancreatic juices contain several inactive precursors of endopeptidases or peptide chain cutting enzymes. These include trypsinogen, chymotrypsinogens A and B, a component of pro-carboxypeptidase similar to chymotrypsinogen and pro-elastase. Once activated in the duodenum these enzymes have different specificities to the side chain immediately preceding the peptide bond to be cleaved. Trypsin is highly specific toward the binding of positively charged side chains of lysine and arginine, while chymotrypsin and elastase have specificity toward large hydrophobic and small aliphatic side chains, respectively.
The known tertiary structures of α-chymotrypsin (Birktoft et al., 1970), γ-chymotrypsin (Davies et al., 1969), chymotrypsinogen (Freer et al., 1970), elastase (Watson et al., 1970), and trypsin (Stroud et al., 1970) demonstrate the very close architectural similarity between the pancreatic serine proteases expected on the basis of sequence homologies (Sigler et al., 1968; Walsh and Neurath, 1964; Hartley et al., 1965). We should therefore like to defer
