General Information

    • DRAMP ID

    • DRAMP03798

    • Peptide Name

    • Corticostatin-related peptide RK-1 (RK-1; lagomorphs, mammals, animals)

    • Source

    • Oryctolagus cuniculus (Rabbit)

    • Family

    • Belongs to the alpha-defensin family

    • Gene

    • Not found

    • Sequence

    • MPCSCKKYCDPWEVIDGSCGLFNSKYICCREK

    • Sequence Length

    • 32

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram-

    • Target Organism

      • Gram-negative bacterium: Escherichia coli.

    • Hemolytic Activity

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

    • 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 Cys3 and Cys29,Cys5 and Cys19,Cys9 and Cys28.

    • Stereochemistry

    • L

    • Structure

    • Beta strand(3 strands; 13 residues)

    • Structure Description

    • RK-1 consists of 32 residues, including six cysteines arranged into three disulfide bonds. The three-dimensional solution structure, determined by NMR, consists of a triple-stranded antiparallel beta-sheet and a series of turns and is similar to the known structures of other alpha-defensins (Ref.3).

    • Helical Wheel Diagram

    • DRAMP03798 helical wheel diagram

    • PDB ID

    • 1EWS resolved by NMR.

    • Predicted Structure

    • There is no predicted structure for DRAMP03798.

Physicochemical Information

    • Formula

    • C159H245N41O47S7

    • Absent Amino Acids

    • AHQT

    • Common Amino Acids

    • C

    • Mass

    • 3707.36

    • PI

    • 7.54

    • Basic Residues

    • 5

    • Acidic Residues

    • 4

    • Hydrophobic Residues

    • 6

    • Net Charge

    • +1

    • Boman Index

    • -49.28

    • Hydrophobicity

    • -0.338

    • Aliphatic Index

    • 45.63

    • Half Life

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

    • Extinction Coefficient Cystines

    • 8855

    • Absorbance 280nm

    • 285.65

    • Polar Residues

    • 14

DRAMP03798

DRAMP03798 chydropathy plot

Comments Information

    • Function

    • Has antimicrobial activity against Escherichia coli and activates Ca(2+) channels in vitro.

    • PTM

    • Contains three disulfide bonds 3-29; 5-19; 9-28.

Literature Information

  • ·Literature 1

    • Title

    • The isolation and characterization of a novel corticostatin/defensin-like peptide from the kidney.

    • Reference

    • J Biol Chem. 1996 May 3;271(18):10654-10659.

    • Author

    • Bateman A, MacLeod RJ, Lembessis P, Hu J, Esch F, Solomon S.
  • ·Literature 2

    • Title

    • Three-dimensional structure of RK-1: a novel alpha-defensin peptide.

    • Reference

    • Biochemistry. 2000 Dec 26;39(51):15757-15764.

    • Author

    • McManus AM, Dawson NF, Wade JD, Carrington LE, Winzor DJ, Craik DJ.