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 |
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| PPepDB ID | PPepDB_3968 |
| Peptide Name | Pa-AMP1 (PAFP-S) |
| PMID(s) | 10759497, 10082954 |
| Plant Source (Scientific Name) | Phytolacca americana |
| Plant Source (Common Name) | Virginian pokeweed |
| Plant Family | Phytolaccaceae |
| Peptide Family | Knottin |
| Peptide Function | Antibacterial, Antifungal |
| Peptide Function Description | possesses antifungal activity; Target site- Lipid Bilayer |
| Activity Against | Gram-positive bacteria: Bacillus megaterium (IC50= 8 µg/mL), Staphyanococcus sp. (IC50= 11 µg/mL). NOTE! not active against Escherichia coli. Fungi: Alternaria panax, Fusarium sp., Rhizoctonia solani. |
| IC50 value | 8 µg/mL | 11 µg/mL |
| Sequence | AGCIKNGGRCNASAGPPYCCSSYCFQIAGQSYGVCKNR |
| Sequence Length | 38 |
| Validation | Experimental evidence at protein level |
| Average Molecular Weight (Da) | 3935.47 |
| Monoisotopic Molecular Weight (Da) | 3932.71 |
| Isoelectric Point (pI) | 8.9 |
| Method / Extraction | NMR |
| External links (Uniprot, PDB and Source Information Database) |
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| Uniprot | P81418, O82728 |
| NCBI | 6226952 |
| EMBL | --NA-- |
| Link to Source Databases | PhytAMP_PHYT00273, DBAASP_5107, EROP-Moscow_02407, CAMPSQ565, APD_00916, APD_00479 |
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| Addtional Information | It contains three disulfide bonds: 3,20; 10,24; 19,35.The global fold involves a cystine-knotted three-stranded antiparallel beta-sheet (residues 8-10, 23-27, 32-36), a flexible loop (residues 14-19), and four beta-reverse turns (residues 4-8, 11-14, 19-22, 28-32). This structure features all the characteristics of the knottin fold. It is the first structural model of an antifungal peptide that adopts a knottin-type structure (Gao et al., 2001). You can rotate, zoom, and view the 3D structure here in the PDB . A hydrophobic surface, comprising Y23, F25, I27, Y32, and V34, is bordered by basic R9, K36, and R38. Such a structural feature may be important for antimicrobial activity. Updated 11/2011; 2/2014; 8/2015 GW. |
