Detailed Peptide Information
This page shows detailed information of individual peptides present in PlantPepDB database. The page is majorly divided into 3 sections. The first sections contains primary information like peptide activity, source, sequence, etc. In the secondary information section user can access the tertiary structure as well as the physico-chemical properties by clicking the respective links. Further there is also link of the source database and research article from which the peptide data is retrieved. Download the information by clicking
| Primary Information |
|---|
| PPepDB ID | PPepDB_264 |
| Peptide Name | Jaburetox-2Ec |
| PMID(s) | --NA-- |
| Plant Source (Scientific Name) | Canavalia ensiformis |
| Plant Source (Common Name) | Jack bean, Horse bean |
| Plant Family | Fabaceae |
| Peptide Family | fragment of canatoxin |
| Peptide Function | Antifungal, Insecticidal |
| Peptide Function Description | --NA-- |
| Activity Against | --NA-- |
| IC50 value | --NA-- |
| Sequence | MGPVNEANCKAAMEIVCRREFGHKEEEDASEGVTTGDPDCPFTKAIPREEYANKYGPTIGDKIRLGDTDLIAEIEKDFALYGDESVFGGGKVI |
| Sequence Length | 93 |
| Validation | Experimental evidence at protein level |
| Average Molecular Weight (Da) | 10128.29 |
| Monoisotopic Molecular Weight (Da) | 10121.85 |
| Isoelectric Point (pI) | 4.48 |
| Method / Extraction | NMR |
| External links (Uniprot, PDB and Source Information Database) |
|---|
| Uniprot | --NA-- |
| NCBI | --NA-- |
| EMBL | --NA-- |
| Link to Source Databases | APD_02628 |
|---|
| Addtional Information | APD analysis reveals that the sequence of this peptide most resembles (43.6% similarity) Mj-AMP2. Mol Wt: 10098.318; mol formula: C440H690N114O147S5; GRAVY: -0.53. Its toxicity relies on an internal 10 kDa peptide (pepcanatox), released by hydrolysis of Canatoxin by cathepsins in the digestive system of susceptible insects. Shown here is the 93 amino acid fragment recombinantly expressed for biological and structural analysis (The six-residue His tag was omitted). It is insecticidal (e.g. S. frugiperda larvae). In 2012, it was shown to also inhibit fungi such as S. cerevisiae, C. parapsilosis, P. membranisfaciens at 9 uM and yeasts, C. tropicalis, K. marxiannus and C. albicans at 18 uM (Postal M et al., 2012). Membane permeation is the likely mechanism for inhibiting both insects and fungi. It seems that the N-terminal 44 residues are more important than the C-terminal portion (Martinelli AH et al., 2014). A helical region was found at the N-terminus. However, the peptide is largely diosordered, consistent with (15)N relaxation studies that revealed significant backbone mobility, especially in the N-terminal portion of the polypeptide (Lopes FC et al., 2015). |
