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 IDPPepDB_2147
Peptide NameEcAMP1
PMID(s)21561864, 24275143
Plant Source (Scientific Name)Echinochloa crus-galli
Plant Source (Common Name)Cockspur grass
Plant FamilyPoaceae
Peptide FamilyHairpin-like peptide
Peptide FunctionAntifungal, Anti-protist, Antimicrobial
Peptide Function DescriptionTarget site: lipid bilayer
Activity AgainstAlternaria alternata (EC50: 16.0 ±2.3 µM), Alternaria solani (EC50: 14.0 ±2.1 µM), Aspergillus niger (EC50: >32 µM), Bipolaris sorokiniana (EC50: 18.2 ±2.7 µM), Colletotrichum graminicola (EC50: >10 µM), Diplodia maydis (EC50: >10 µM), Fusarium graminearum (EC50: 4.5 ±1.4 µM), Fusarium oxysporum (EC50: 8.5 ±1.6 µM), Fusarium solani (EC50: 4.0 ±1.2 µM), Fusarium verticillioides (EC50: 8.1 ±2.3 µM), Phoma betae (EC50: 6.0 ±1.5 µM), Phytophthora infestans (EC50: 16.3 ±2.5 µM), Pythium debaryanum (EC50: 12.0 ±1.7 µM), Pythium ultimum (EC50: 14.4 ±2.1 µM), Trichoderma album (EC50: >32 µM), Pseudomonas syringae (MIC: 24.0 µM), Clavibacter michiganensis subsp. michiganensis (MIC: 24.0 µM), Erwinia carotovora subsp. carotovora (MIC: 11.9 µM), Fusarium graminearum (IC50: 4.5 µM), Fusarium oxysporum (IC50: 8.5 µM), Aspergillus niger (IC50: >32.0 µM), Bipolaris sorokiniana (IC50: 18.2 µM)
IC50 value4.5 µM | 8.5 µM | >32.0 µM | 18.2 µM
SequenceGSGRGSCRSQCMRRHEDEPWRVQECVSQCRRRRGGGD
Sequence Length37
ValidationExperimental evidence at protein level
Average Molecular Weight (Da)4278.73
Monoisotopic Molecular Weight (Da)4275.94
Isoelectric Point (pI)9.47
Method / ExtractionNMR


Secondary Information
Tertiary Structure and DSSP ReportClick to View Structure
Physico-Chemical Properties of peptidesClick to View Physico-Chemical Details of PPepDB_2147


External links (Uniprot, PDB and Source Information Database)
UniprotP86698, V5TB87, V5TAQ7, V5TA00, V5T9K0, V5TB82, V5T9J5, B3EWR6
NCBI--NA--
EMBL--NA--
Link to Source DatabasesDBAASP_4291, EROP-Moscow_11393, CAMPSQ3483, APD_01760
Addtional InformationSynthesis Type : Ribosomal; There are two disulfide bonds (C7-C29 and C11-C25) that tie the two helices together into a unique beta hairpin structure. Other more sophisticated disulfide bond stabilized helical structures include distinctin and several saposin-like AMPs such as porcine NK-lysin and caenopore-5. MOA: EcAMP1 binds to fungal surface followed by internalization without disrupting membranes. You can rotate, zoom, and view the 3D structure here in the PDB. Updated 9/19/11. GW