A simple fold with variations: The pacifastin inhibitor family

Research output: Article

14 Citations (Scopus)

Abstract

Members of the pacifastin family are small, ∼35-residue serine protease inhibitors isolated from arthropod species. Several locust inhibitors exhibit intriguing taxon specificity while others do not. The structural basis of this phenomenon may lie in the different dynamical properties of the proteins originating from different stabilizing interactions. In this study, we identify new members of the family to confirm the universal role of these interactions in the family. Structural investigations show that both the disulfide pattern and the stabilizing interactions are unique among small all-beta proteins.

Original languageEnglish
Pages (from-to)448-451
Number of pages4
JournalBioinformatics
Volume20
Issue number4
DOIs
Publication statusPublished - márc. 1 2004

ASJC Scopus subject areas

  • Statistics and Probability
  • Biochemistry
  • Molecular Biology
  • Computer Science Applications
  • Computational Theory and Mathematics
  • Computational Mathematics

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