Characterization of a new member of kunitz-type protein family from the venom of Persian false-horned viper, Pseudocerastes persicus
| Autor: | Seyede Elnaz Banijamali, Mehriar Amininasab, Mitra Maryam Elmi |
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| Rok vydání: | 2019 |
| Předmět: |
Models
Molecular 0301 basic medicine Protein family Trypsin inhibitor Biophysics Dendrotoxin Viper Venoms Biochemistry 03 medical and health sciences Viperidae medicine Animals Trypsin Amino Acid Sequence Homology modeling Molecular Biology chemistry.chemical_classification Molecular Structure 030102 biochemistry & molecular biology Amino acid 030104 developmental biology chemistry Snake venom Proteolysis Kunitz domain Trypsin Inhibitors medicine.drug |
| Zdroj: | Archives of Biochemistry and Biophysics. 662:1-6 |
| ISSN: | 0003-9861 |
| DOI: | 10.1016/j.abb.2018.11.017 |
| Popis: | A new member of kunitz-type protein family, PPTI (Pseudocerastes Persicus Trypsin Inhibitor), was isolated from the venom of Persian false horned viper Pseudocerastes persicus and characterized. Mass spectrometry and amino acid sequencing revealed that PPTI is a 68 amino acid protein with molecular weight of about 7.6 kDa. The first amino acid residue of PPTI is N-terminally blocked via a post translational modification to pyroglutamyl. Sequence comparison against UniProtKB shows a high sequence similarity of PPTI with kunitz-type proteins, especially serine protease inhibitors and dendrotoxins (DTXs). The number of cysteines and disulfide bonding pattern of PPTI are the same as kunitz-type proteins. Based on sequence derive information, anti-protease activity of PPTI against trypsin was experimentally examined. The constructed homology models of PPTI confirmed the ability of PPTI to fold similarly to kunitz domain. The presence of characteristic basic-hydrophobic functional dyad of DTXs in PPTI supports its inhibitory potential against potassium channels. In summary, this study hypothesized the dual functionality of PPTI according to its inhibitory effect on trypsin and its potential ability in blocking potassium channel. |
| Databáze: | OpenAIRE |
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