Kunitz-type soybean trypsin inhibitor revisited: refined structure of its complex with porcine trypsin reveals an insight into the interaction between a homologous inhibitor from Erythrina caffra and tissue-type plasminogen activator.

@article{Song1998KunitztypeST,
  title={Kunitz-type soybean trypsin inhibitor revisited: refined structure of its complex with porcine trypsin reveals an insight into the interaction between a homologous inhibitor from Erythrina caffra and tissue-type plasminogen activator.},
  author={H. K. Song and Se Won Suh},
  journal={Journal of molecular biology},
  year={1998},
  volume={275 2},
  pages={
          347-63
        }
}
  • H. SongS. Suh
  • Published 16 January 1998
  • Chemistry
  • Journal of molecular biology
The Kunitz-type trypsin inhibitor from soybean (STI) consists of 181 amino acid residues with two disulfide bridges. Its crystal structures have been determined in complex with porcine pancreatic trypsin in two crystal forms (an orthorhombic form at 1.75 A resolution and a tetragonal form at 1.9 A) and in the free state at 2.3 A resolution. They have been refined to crystallographic R-values of 18.9%, 21.6% and 19.8%, respectively. The three models of STI reported here represent a significant… 

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References

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In the resulting electron density maps the trypsin molecule was easily identifiable, and although some parts of the inhibitor were not clear, a precise interpretation of residues 1'-93' was made, including the con- tact region.

Refined 1.6 A resolution crystal structure of the complex formed between porcine beta-trypsin and MCTI-A, a trypsin inhibitor of the squash family. Detailed comparison with bovine beta-trypsin and its complex.

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