• DRAMP ID

    • DRAMP02980
    • Peptide Name

    • Antimicrobial peptide NK-lysin (NKL; pigs, mammals, animals)
    • Source

    • Sus scrofa (Pig)
    • Family

    • Not found
    • Gene

    • NKL
    • Sequence

    • GLICESCRKIIQKLEDMVGPQPNEDTVTQAASRVCDKMKILRGVCKKIMRTFLRRISKDILTGKKPQAICVDIKICKE
    • Sequence Length

    • 78
    • Protein Existence

    • Protein level
    • Biological Activity

    • Antimicrobial, Antibacterial, Antifungal, Antitumor
    • Target Organism

      • [with medium E]: Escherichia coli D21 (MIC=0.5 µM), Escherichia coli Bd2221/75 (MIC=10 µM), Acinetobacter calcoaceticus Ac 11 (MIC=7 µM), Bacillus megaterium Bmll (MIC=1.6 µM);
      • [without medium E]: Escherichia coli D21 (MIC=8 µM), Escherichia coli Bd2221/75 (MIC=39 µM), Bacillus megaterium Bmll (MIC=0.8 µM), Streptococcus pyogenes w.t. (MIC=34 µM), Candida albicans w.t. (MIC=31 µM).
    • Hemolytic Activity

      • [Ref.7737114] It exhibits no hemolytic activity at 170 µM against sheep red blood cells.
    • Cytotoxicity

      • [Ref.7737114] NK-lysin at 50μg/ml was able to give 90% lysis of 5'Cr-labelled YAC-1 cells in a medium with 2% fetal calf serum(FCS) and 75% lysis in phosphate-buffered saline(PBS), 15% lysis suspended in medium E.
    • Binding Target

    • Lipopolysaccharide (LPS)-binding
    • Linear/Cyclic

    • Cyclic
    • N-terminal Modification

    • Free
    • C-terminal Modification

    • Free
    • Nonterminal Modifications and Unusual Amino Acids

    • Disulfide bonds between Cys4 and Cys76; Cys7 and Cys70; Cys35 and Cys45.
    • Stereochemistry

    • L
    • Structure

    • Alpha helix
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP02980 helical wheel diagram
    • PDB ID

    • 1NKL resolved by NMR.
    • Predicted Structure

    • There is no predicted structure for DRAMP02980.
    • Formula

    • C380H664N112O109S9
    • Absent Amino Acids

    • HWY
    • Common Amino Acids

    • KI
    • Mass

    • 8834.68
    • PI

    • 9.47
    • Basic Residues

    • 17
    • Acidic Residues

    • 9
    • Hydrophobic Residues

    • 24
    • Net Charge

    • +8
    • Boman Index

    • -149.79
    • Hydrophobicity

    • -0.213
    • Aliphatic Index

    • 97.44
    • Half Life

      • Mammalian:30 hour
      • Yeast:>20 hour
      • E.coli:>10 hour
    • Extinction Coefficient Cystines

    • 375
    • Absorbance 280nm

    • 4.87
    • Polar Residues

    • 18

DRAMP02980

DRAMP02980 chydropathy plot
    • Function

    • May be an effector molecule of cytotoxic activity. High activity against E. coli and B. megaterium, moderate against A. calcoaceticus and S. pyogenes. Has some antifungal activity against Candida albicans.
    • Tissue specificity

    • Cytotoxic T and NK cells. Induction
    • PTM

    • Contains three disulfide bonds 4-76; 7-70; 35-45.
  • ·Literature 1
    • Title

    • NK-lysin, a novel effector peptide of cytotoxic T and NK cells. Structure and cDNA cloning of the porcine form, induction by interleukin 2, antibacterial and antitumour activity.
    • Reference

    • EMBO J. 1995 Apr 18;14(8):1615-1625.
    • Author

    • Andersson M, Gunne H, Agerberth B, Boman A, Bergman T, Sillard R, Jörnvall H, Mutt V, Olsson B, Wigzell H, et al.
  • ·Literature 2
    • Title

    • Saposin fold revealed by the NMR structure of NK-lysin.
    • Reference

    • Nat Struct Biol. 1997 Oct;4(10):793-795.
    • Author

    • Liepinsh E, Andersson M, Ruysschaert JM, Otting G.