Structure-activity relationship within the serine protease inhibitors of the pacifastin family

Protein Pept Lett. 2005 Jul;12(5):409-14. doi: 10.2174/0929866054395239.

Abstract

The members of the Pacifastin family are serine protease inhibitors found in insects and crustacean. They are either small inhibitors (made of one consensus cysteine-rich motif) or proteins (4-9 motifs). Some of these inhibitors are characterized by a species selectivity for the trypsin inhibition. Structural data discriminate the small inhibitors that apparently look very similar into two groups. Interestingly, the inhibitors that display species selectivity fall in the same structural group.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Crustacea / enzymology
  • Insecta / enzymology
  • Molecular Sequence Data
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Proteins / chemistry
  • Proteins / metabolism*
  • Serine Proteinase Inhibitors / chemistry
  • Serine Proteinase Inhibitors / metabolism*
  • Structure-Activity Relationship

Substances

  • Proteins
  • Serine Proteinase Inhibitors
  • pacifastin