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Updated: May 14, 2026

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
Published on: July 25, 2013
A simple fold with variations: the pacifastin inhibitor family
Zoltán Gáspári1, Csaba Ortutay, András Perczel
1Department of Organic Chemistry, Eötvös University, Pázmány Péter sétány 1/A, Budapest, Hungary. szpari@para.chem.elte.hu
Abstract:
Members of the pacifastin family are small, approximately 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.
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