A simple fold with variations: the pacifastin inhibitor family | Zendy

Zoltán Gáspári | Zendy; Csaba Ortutay | Zendy; András Perczel | Zendy

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A simple fold with variations: the pacifastin inhibitor family

Author(s) -

Zoltán Gáspári,

Csaba Ortutay,

András Perczel

Publication year - 2004

Publication title -

bioinformatics

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.599

H-Index - 390

eISSN - 1367-4811

pISSN - 1367-4803

DOI - 10.1093/bioinformatics/btg451

Subject(s) - fold (higher order function) , simple (philosophy) , computer science , algorithm , programming language , philosophy , epistemology

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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