General Information

    • DRAMP ID

    • DRAMP03598

    • Peptide Name

    • Human beta-defensin 2 (hBD-2; Defensin, beta 2; Beta-defensin 4A; Human, mammals, animals)

    • Source

    • Homo sapiens (Human)

    • Family

    • Belongs to the beta-defensin family

    • Gene

    • DEFB4A AND DEFB4B

    • Sequence

    • GIGDPVTCLKSGAICHPVFCPRRYKQIGTCGLPGTKCCKKP

    • Sequence Length

    • 41

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antiviral

    • Target Organism

      • Gram-negative bacteria: Escherichia coli D31(MIC=62 µg/ml), Escherichia coli ATCC (MIC=62 µg/ml), Pseudomonas aeruginosa ATCC (MIC=62 µg/ml);
      • Gram-positive bacteria: Staphylococcus aureus ATCC (MIC=62 µg/ml), Enterococcus faecalis ATCC (MIC=15 µg/ml).

    • Hemolytic Activity

      • [Ref.15625724] It is slightly hemolytic (<12%) against human erythrocytes at the highest concentration of 500 μg/ml.

    • 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 Cys8 and Cys37,Cys15 and Cys30,Cys20 and Cys38.

    • Stereochemistry

    • L

    • Structure

    • Combine helix and strand structure

    • Structure Description

    • The structure (one N-terminal helix and 3 beta strands) was found to be monomer in solution (PDB ID: 1E4Q) but a dimer in the crystal (PDB ID: 1FD3).

    • Helical Wheel Diagram

    • DRAMP03598 helical wheel diagram

    • Predicted Structure

    • There is no predicted structure for DRAMP03598.

Physicochemical Information

    • Formula

    • C188H311N55O50S6

    • Absent Amino Acids

    • EMNW

    • Common Amino Acids

    • CG

    • Mass

    • 4334.24

    • PI

    • 9.3

    • Basic Residues

    • 8

    • Acidic Residues

    • 1

    • Hydrophobic Residues

    • 9

    • Net Charge

    • +7

    • Boman Index

    • -36.97

    • Hydrophobicity

    • -0.102

    • Aliphatic Index

    • 64.15

    • Half Life

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

    • Extinction Coefficient Cystines

    • 1865

    • Absorbance 280nm

    • 46.63

    • Polar Residues

    • 17

DRAMP03598

DRAMP03598 chydropathy plot

Comments Information

    • Function

    • Has anti-HIV and antibacterial activity.

    • Tissue specificity

    • Expressed in the skin and respiratory tract.

    • Induction

    • By inflammation.

    • PTM

    • Contains three disulfide bonds 8-37, 15-30, 20-38.

    • Transgenic plants

    • expression of this peptide in Arabidopsis thaliana reduced fungal infection.

Literature Information

  • ·Literature 1

    • Title

    • A peptide antibiotic from human skin.

    • Reference

    • Nature. 1997 Jun 26;387(6636):861.

    • Author

    • Harder J, Bartels J, Christophers E, Schröder JM.
  • ·Literature 2

    • Title

    • The structure of human beta-defensin-2 shows evidence of higher order oligomerization.

    • Reference

    • J Biol Chem. 2000 Oct 20;275(42):32911-32918.

    • Author

    • Hoover DM, Rajashankar KR, Blumenthal R, Puri A, Oppenheim JJ, Chertov O, Lubkowski J.
  • ·Literature 3

    • Title

    • Arabidopsis thaliana plants expressing human beta-defensin-2 are more resistant to fungal attack: functional homology between plant and human defensins.

    • Reference

    • Plant Cell Rep. 2007 Aug;26(8):1391-1398.

    • Author

    • Aerts AM, Thevissen K, Bresseleers SM, Sels J, Wouters P, Cammue BP, François IE.