A simple fold with variations: the pacifastin inhibitor family.
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.
Department of Organic Chemistry, Eötvös University, Pázmány Péter sétány 1/A, Budapest, Hungary. szpari@para.chem.elte.hu
Zoltán
Z
Gáspári
Csaba
C
Ortutay
András
A
Perczel
D001665:Binding Sites; D003198:Computer Simulation; D020224:Expressed Sequence Tags; D008958:Models, Molecular; D010802:Phylogeny; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000235:genetics; D016415:Sequence Alignment / Q000379:methods*; D020539:Sequence Analysis, Protein / Q000379:methods*; D017386:Sequence Homology, Amino Acid; D015842:Serine Proteinase Inhibitors / Q000737:chemistry* / Q000235:genetics; D013045:Species Specificity; D013329:Structure-Activity Relationship
D011506:Proteins; D015842:Serine Proteinase Inhibitors; C106709:pacifastin