General Information

    • DRAMP ID

    • DRAMP02644

    • Peptide Name

    • Rhesus theta-defensin 3 (RTD-3; primates, mammals, animals)

    • Source

    • Macaca mulatta (Rhesus macaque)

    • Family

    • Belongs to the alpha-defensin family (Theta subfamily)

    • Gene

    • Not found

    • Sequence

    • RCICTRGFCRCICTRGFC

    • Sequence Length

    • 18

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

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

    • Target Organism

      • Gram-positive bacteria: Staphylococcus aureus 502a, Listeria monocytogenes;
      • Gram-negative bacteria: Salmonella typhimurium, Escherichia coli ML35.
      • Fungi: Candida albicans 16820, Cryptococcus neoformans 271A (the activity of RTD-2 against Escherichia coli ML35 was 2-3-fold less than those of RTD-1 and RTD-3).

    • Hemolytic Activity

      • No hemolysis information or data found in the reference(s) presented in this entry

    • Cytotoxicity

      • Not included yet

    • Binding Target

    • Not found

Structure Information

    • Linear/Cyclic

    • Not included yet

    • N-terminal Modification

    • Not included yet

    • C-terminal Modification

    • Not included yet

    • Nonterminal Modifications and Unusual Amino Acids

    • Not included yet

    • Stereochemistry

    • Not included yet

    • Structure

    • Bridge

    • Structure Description

    • Not found

    • Helical Wheel Diagram

    • DRAMP02644 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

    • There is no predicted structure for DRAMP02644.

Physicochemical Information

    • Formula

    • C84H140N30O21S6

    • Absent Amino Acids

    • ADEHKLMNPQSVWY

    • Common Amino Acids

    • C

    • Mass

    • 2098.58

    • PI

    • 9.01

    • Basic Residues

    • 4

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 4

    • Net Charge

    • +4

    • Boman Index

    • -39.46

    • Hydrophobicity

    • 0.522

    • Aliphatic Index

    • 43.33

    • Half Life

      • Mammalian:1 hour
      • Yeast:2 min
      • E.coli:2 min

    • Extinction Coefficient Cystines

    • 375

    • Absorbance 280nm

    • 22.06

    • Polar Residues

    • 10

DRAMP02644

DRAMP02644 chydropathy plot

Comments Information

    • Function

    • RTD-1 and RTD-3 have similar antimicrobial activities against the Gram-positive bacteria, the Gram-negative bacteria and the fungi C. albicans 16820 and C. neoformans 271A.

    • Subunit structure RTD-1 is a cyclic heterodimer composed of subunits A and B; disulfide-linked. RTD-3 is a cyclic homodimer composed of two subunits A; disulfide-linked.

    • PTM

    • Forms a cyclic peptide with subunit A (RTD-3) or with subunit B (RTD-1). An additional intersubunit disulfide bond is formed.

    • Miscellaneous

    • RTD-1 is 10-fold more present in cells than RTD-3.

Literature Information

  • ·Literature 1

    • Title

    • A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated alpha-defensins.

    • Reference

    • Science. 1999 Oct 15;286(5439):498-502.

    • Author

    • Tang YQ, Yuan J, Osapay G, Osapay K, Tran D, Miller CJ, Ouellette AJ, Selsted ME.
  • ·Literature 2

    • Title

    • Circular minidefensins and posttranslational generation of molecular diversity.

    • Reference

    • J Leukoc Biol. 2001 Sep;70(3):461-464.

    • Author

    • Leonova L, Kokryakov VN, Aleshina G, Hong T, Nguyen T, Zhao C, Waring AJ, Lehrer RI.
  • ·Literature 3

    • Title

    • Homodimeric theta-defensins from rhesus macaque leukocytes: isolation, synthesis, antimicrobial activities, and bacterial binding properties of the cyclic peptides.

    • Reference

    • J Biol Chem. 2002 Feb 1;277(5):3079-3084.

    • Author

    • Tran D, Tran PA, Tang YQ, Yuan J, Cole T, Selsted ME.