Name
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. |
Year | DOI | Venue |
|---|---|---|
2004 | 10.1093/bioinformatics/btg451 | Bioinformatics |
Keywords | Field | DocType |
detailed description,structural investigation,structural basis,intriguing taxon specificity,disulfide pattern,small all-beta protein,pacifastin inhibitor family,35-residue serine protease,pacifastin family,arthropod species,different dynamical property | Locust,Enzyme,Biology,Disulfide bond,Serine Protease Inhibitors,Arthropod,Bioinformatics,Web site,Pacifastin | Journal |
Volume | Issue | ISSN |
20 | 4 | 1367-4803 |
Citations | PageRank | References |
1 | 0.78 | 0 |
Authors | ||
3 | ||
Name | Order | Citations | PageRank |
|---|---|---|---|
| Zoltán Gáspári | 1 | 38 | 5.46 |
| Csaba Ortutay | 2 | 6 | 1.38 |
| András Perczel | 3 | 39 | 16.63 |