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_2067
Peptide NameDefensin 4, MtDef4
PMID(s)21533249
Plant Source (Scientific Name)Medicago truncatula
Plant Source (Common Name)Barrelclover
Plant FamilyFabaceae
Peptide FamilyDefensin
Peptide FunctionAntifungal
Peptide Function DescriptionTarget site- Lipid Bilayer
Activity AgainstFusarium graminearum (IC50: 0.75-1 µM), Fusarium graminearum (MIC: 1.5-2.5 µM)
IC50 value0.75-1 µM
SequenceRTCESQSHKFKGPCASDHNCASVCQTERFSGGRCRGFRRRCFCTTHC
Sequence Length47
ValidationExperimental evidence at protein level
Average Molecular Weight (Da)5343.03
Monoisotopic Molecular Weight (Da)5339.34
Isoelectric Point (pI)9.17
Method / ExtractionNMR


Secondary Information
Tertiary Structure and DSSP ReportClick to View Structure
Physico-Chemical Properties of peptidesClick to View Physico-Chemical Details of PPepDB_2067


External links (Uniprot, PDB and Source Information Database)
UniprotG7L736
NCBI--NA--
EMBL--NA--
Link to Source DatabasesDBAASP_9212, APD_02428
Addtional InformationSynthesis Type: Ribosomal; In UniProt 33th amino acid is H instead of R; Active against fungus F. graminearum that causes head blight disease in cereals. MtDef4 binds to phosphatidic acid (PA). PA is a precursor for lipid biosynthesis and a signaling molecule that recruits cytosolic proteins to membranes. You can rotate, zoom, and view the NMR structure 2LR3 here in the PDB. MOA: MtDef4 rapidly permeabilizes fungal plasma membrane and is internalized by the fungal cells where it accumulates in the cytoplasm (see the structure paper PDB). THe sequence RGFRRR is likely the translolcation signal. Note that amino acid substitutions in the RGFRRR sequence not only abolished the ability of MtDef4 to enter fungal cells but also impaired its ability to bind PA. Updated 3/2015.