• • DRAMP ID

  • DRAMP02643

• • Peptide Name

  • Rhesus theta-defensin 2 (RTD-2; primates, mammals, animals)

• • Source

  • Macaca mulatta (Rhesus macaque)

• • Family

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

• • Gene

  • Not found

• • Sequence

  • RCLCRRGVCRCLCRRGVC

• • Sequence Length

  • 18

• • UniProt Entry

  • P82271

• • Protein Existence

  • Protein level

• • Biological Activity

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

• • 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

• • 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

  • 

• • PDB ID

  • None

• Predicted Structure

• There is no predicted structure for DRAMP02643.

DRAMP02643

• • Function

  • RTD-1 and RTD-2 have similar antimicrobial activities against the Gram-positive bacteria S. aureus 502A and L. monocytogenes, the Gram-negative bacterium S. typhimurium, and the fungi C. albicans 16820 and C. neoformans 271A. RTD-2 is 2-3-fold less active than RTD-1 against E. coli ML35.

• • Subunit structure

  • RTD-2 is a cyclic homodimer composed of two subunits B; disulfide-linked.

• • PTM

  • Forms a cyclic peptide with 1 subunit B (RTD-2) or with 1 subunit A (RTD-1). An additional intersubunit disulfide bond is formed.

• • Miscellaneous

  • RTD-1 is 10-fold more present in cells than RTD-2.

• ·Literature 1

• • Title

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

• • Pubmed ID

  • 10521339

• • 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.

• • Pubmed ID

  • 1152799

• • 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.

• • Pubmed ID

  • 11675394

• • Reference

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

• • Author

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