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.

  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},
  volume={275 2},
  • 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… 

Structural insights into the unique inhibitory mechanism of Kunitz type trypsin inhibitor from Cicer arietinum L.

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Crystal structure analysis of the complex of soybean trypsin inhibitor (Kunitz) (STI), one of the largest inhibitors, with porcinetrypsin, improves the understanding of the catalytic mechanism of trypsine, and provides insight into the development of strong, specific binding between protein molecules.

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