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Bioinformatics Advance Access originally published online on January 22, 2004
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Bioinformatics 20(4) © Oxford University Press 2004; all rights reserved.

Discovery Note

A simple fold with variations: the pacifastin inhibitor family

Zoltán Gáspári 1,*, Csaba Ortutay 2 and András Perczel 1

1 Department of Organic Chemistry, Eötvös University, Pázmány Péter sétány 1/A and 2 Department of Genetics, Eötvös University, Pázmány Péter sétány 1/C, 1117 Budapest, Hungary

Received on June 10, 2003 ; revised on September 30, 2003 ; accepted on October 1, 2003
Advance Access Publication January 22, 2004

Summary: 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.

Availability: Detailed description of the results can be found at http://www.chem.elte.hu/departments/protnmr/pif

Contact: szpari{at}para.chem.elte.hu

* To whom correspondence should be addressed.


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