• DRAMP ID

    • DRAMP03599
    • Peptide Name

    • Human beta-defensin 3 (BD-3, hBD-3; Hbd3; Beta-defensin 103; Human, mammals, animals)
    • Source

    • Homo sapiens (Human)
    • Family

    • Belongs to the beta-defensin family
    • Gene

    • DEFB103A AND DEFB103
    • Sequence

    • GIINTLQKYYCRVRGGRCAVLSCLPKEEQIGKCSTRGRKCCRRKK
    • Sequence Length

    • 45
    • Protein Existence

    • Protein level
    • Biological Activity

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

      • [Ref.11085990]Gram-negative bacteria: Escherichia coli DSM1103 (MIC=9.4 µg/ml), Klebsiella pneumoniae DSM681 (MIC=25 µg/ml), Pseudomonas aeruginosa DSM1128 (MIC=18.75 µg/ml);
      • Gram-positive bacteria: Staphylococcus aureus ATCC25923 (MIC=4.7 µg/ml), Streptococcus pneumoniae DSM11865 (MIC=4.7 µg/ml).
    • Hemolytic Activity

      • [Ref.11085990] It has 9% hemolysis at 250 µg/ml, 15% hemolysis at 500 µg/ml against human erythrocytes.
    • Cytotoxicity

    • No cytotoxicity information found in the reference(s) presented
    • Binding Target

    • Not found
    • Linear/Cyclic

    • Cyclic
    • N-terminal Modification

    • Free
    • C-terminal Modification

    • Free
    • Nonterminal Modifications and Unusual Amino Acids

    • Disulfide bonds between Cys11 and Cys40,Cys18 and Cys33,Cys23 and Cys41.
    • Stereochemistry

    • L
    • Structure

    • Combine helix and strand structure
    • Structure Description

    • Contains three disulfide bonds and a short helical segment preceding a three-stranded antiparallel beta-sheet.
    • Helical Wheel Diagram

    • DRAMP03599 helical wheel diagram
    • PDB ID

    • 1KJ6  resolved by NMR.
    • Predicted Structure

    • Formula

    • C216H377N75O59S6
    • Absent Amino Acids

    • DFHMW
    • Common Amino Acids

    • R
    • Mass

    • 5161.2
    • PI

    • 10.08
    • Basic Residues

    • 13
    • Acidic Residues

    • 2
    • Hydrophobic Residues

    • 9
    • Net Charge

    • +11
    • Boman Index

    • -129.51
    • Hydrophobicity

    • -0.7
    • Aliphatic Index

    • 67.11
    • Half Life

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

    • 3355
    • Absorbance 280nm

    • 76.25
    • Polar Residues

    • 18

DRAMP03599

DRAMP03599 chydropathy plot
    • Function

    • Exhibits antimicrobial activity against Gram-positive bacteria and the Gram-negative bacteria and the yeast C.albicans. Kills multiresistant S. aureus and vancomycin-resistant E. faecium. Has hemolytic activity.
    • Tissue specificity

    • Highly expressed in skin and tonsils, and to a lesser extent in trachea, uterus, kidney, thymus, adenoid, pharynx and tongue. Low expression in salivary gland, bone marrow, colon, stomach, polyp and larynx. No expression in small intestine.
    • Induction

    • By bacterial infection and by IFNG/IFN-gamma.
    • PTM

    • Contains three disulfide bonds 11-40; 18-33; 23-41.
  • ·Literature 1
    • Title

    • Engineering disulfide bonds of the novel human beta-defensins hBD-27 and hBD-28: differences in disulfide formation and biological activity among human beta-defensins.
    • Reference

    • Biopolymers. 2005;80(1):34-49.
    • Author

    • Schulz A, Klüver E, Schulz-Maronde S, Adermann K.
  • ·Literature 2
    • Title

    • Isolation and characterization of human beta-defensin-3, a novel human inducible peptide antibiotic.
    • Reference

    • J Biol Chem. 2001 Feb 23;276(8):5707-5713.
    • Author

    • Harder J, Bartels J, Christophers E, Schroder JM.