General Information

    • 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

Activity Information

    • 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

Structure Information

    • 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

    • There is no predicted structure for DRAMP03599.

Physicochemical Information

    • 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

Comments Information

    • 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 Information

  • ·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.