• DRAMP ID

    • DRAMP00977
    • Peptide Name

    • Antimicrobial peptide 2 (AC-AMP2; Plant defensin)
    • Source

    • Amaranthus caudatus (Love-lies-bleeding) (Inca-wheat)
    • Family

    • N/A
    • Gene

    • N/A
    • Sequence

    • VGECVRGRCPSGMCCSQFGYCGKGPKYCGR
    • Sequence Length

    • 30
    • Evidence code

    • Protein level
    • Biological Activity

    • Antibacterial, Antifungal, Anti-Gram+, Antimicrobial
    • Target Organism

      • Gram-positive bacteria: Bacillus megaterium (IC50=40 µg/ml), Sarcina lutea (IC50=250 µg/ml).
      • Fungi: Alternaria brassicola (IC50=7 µg/ml), Ascochyta pisi (IC50=8 µg/ml), Botrytis cinera (IC50=10 µg/ml), Colletotrichum lindemuthianum (IC50=8 µg/ml), Fusarium culmorum (IC50=2 µg/ml), Trichoderma hamatum (IC50=7 µg/ml), Verticillium dahliae (IC50=6 µg/ml).
    • Hemolytic Activity

      • N/A
    • Cytotoxicity

      • Not included yet
    • Binding Target

    • Chitin-binding
    • Linear/Cyclic

    • Not included yet
    • N-terminal Modification

    • Not included yet
    • C-terminal Modification

    • Not included yet
    • Other Modifications and Unusual Amino Acids

    • Not included yet
    • Stereochemistry

    • Not included yet
    • Structure

    • Beta strand
    • Structure Description

    • The main structural element is an antiparallel beta-sheet from Met13 to Lys23 including a betaI-turn over Gln17-Phel8 with a beta bulge at Gly19. In addition, a beta'I turn over Arg6-Gly7, a beta'III turn over Ser11-Gly12 and a helical turn from Gly24 to Cys28 are identified.
    • DRAMP00977 helical wheel diagram
    • 1MMC-> 
    • Formula

    • C130H206N42O38S7
    • Absent Amino Acids

    • ADHILNTW
    • Common Amino Acids

    • G
    • Mass

    • 3707.19
    • PI

    • 8.62
    • Basic Residues

    • 5
    • Acidic Residues

    • 1
    • Hydrophobic Residues

    • 3
    • Boman Index

    • -47.62
    • Hydrophobicity

    • -34.67
    • Aliphatic Index

    • 19.33
    • Half Life

      • Mammalian:100 hour
      • Yeast:>20 hour
      • E.coli:>10 hour
    • Extinction Coefficient Cystines

    • 3355
    • Absorbance 280nm

    • 115.69
    • Polar Residues

    • 17

DRAMP00977

DRAMP00977 chydropathy plot
    • Function

    • Chitin-binding protein with a defensive Function
    • Miscellaneous

    • Its chitin-binding activity is strongly inhibited by divalent cations.
    • PTM

    • Contains three disulfide bonds 4-15; 9-21; 14-28.
  • Literature 1
    • Title

    • Antimicrobial peptides from Amaranthus caudatus seeds with sequence homology to the cysteine/glycine-rich domain of chitin-binding proteins.
    • Reference

    • Biochemistry. 1992 May 5;31(17):4308-4314.
    • Author

    • Broekaert W.F, Marien W, Terras F.R.G, de Bolle M.F.C, Proost P, van Damme J, Dillen L, Claeys M, Rees S.B, Vanderleyden J, Cammue B.P.A.
  • Literature 2
    • Title

    • H NMR study of the solution structure of Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus.
    • Reference

    • J Mol Biol. 1996 May 3;258(2):322-333.
    • Author

    • Martins JC, Maes D, Loris R, Pepermans HA, Wyns L, Willem R, Verheyden P.
  • Literature 3
    • Title

    • Reference

    • J Pept Res. 1997 Apr;49(4):336-340.
    • Author

    • el Bouyoussfi M, Laus G, Verhey