Analysis of the black-eyed pea trypsin and chymotrypsin inhibitor-alpha-chymotrypsin complex

FEBS Lett. 1997 Jun 9;409(2):121-7. doi: 10.1016/s0014-5793(97)00419-5.

Abstract

The black-eyed pea trypsin and chymotrypsin inhibitor (BTCI) is a member of the Bowman-Birk protease inhibitor (BBI) family. The three-dimensional model of the BTCI-chymotrypsin complex was built based on the homology to Bowman-Birk inhibitors with known structures. An extensive theoretical and experimental study of these known structures has been performed. The model confirms the ideas about Bowman-Birk inhibitor structure-function relations and agrees well with our experimental data (circular dichroism, IR and light scattering). The electrostatic potentials at the enzyme-inhibitor contact surface reveal a pattern of complementary electrostatic potentials from which mutations can be inferred that could give these inhibitors an altered specificity.

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Biopolymers / chemistry
  • Chymotrypsin / antagonists & inhibitors*
  • Crystallography, X-Ray
  • Fabaceae / enzymology*
  • Models, Molecular
  • Molecular Sequence Data
  • Plant Proteins / antagonists & inhibitors
  • Plant Proteins / chemistry*
  • Plants, Medicinal*
  • Sequence Alignment
  • Static Electricity
  • Trypsin / chemistry*
  • Trypsin Inhibitors / chemistry*

Substances

  • Biopolymers
  • Plant Proteins
  • Trypsin Inhibitors
  • Chymotrypsin
  • Trypsin

Associated data

  • PDB/1BB1
  • PDB/1PI2