• DRAMP ID

    • DRAMP02943
    • Peptide Name

    • Tachystatin-B1 (crabs, Arthropods, animals)
    • Source

    • Tachypleus tridentatus (Japanese horseshoe crab)
    • Family

    • Not found
    • Gene

    • Not found
    • Sequence

    • YVSCLFRGARCRVYSGRSCCFGYYCRRDFPGSIFGTCSRRNF
    • Sequence Length

    • 42
    • Protein Existence

    • Protein level
    • Biological Activity

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

      • Gram-positive bacterium: Staphylococcus aureus (IC50=7.4 µg/ml).
      • Fungi: Candida albicans (IC50=3.0 µg/ml), Pichia pastoris (IC50=0.1 µg/ml).
    • Hemolytic Activity

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

      • Not included yet
    • Binding Target

    • Chitin-binding
    • 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

    • Beta strand
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP02943 helical wheel diagram
    • PDB ID

    • 2DCV resolved by NMR.
  • 2DCV-> 
    • Predicted Structure

    • There is no predicted structure for DRAMP02943.
    • Formula

    • C214H319N67O56S6
    • Absent Amino Acids

    • EHKMQW
    • Common Amino Acids

    • R
    • Mass

    • 4918.66
    • PI

    • 9.61
    • Basic Residues

    • 8
    • Acidic Residues

    • 1
    • Hydrophobic Residues

    • 10
    • Net Charge

    • +7
    • Boman Index

    • -107.84
    • Hydrophobicity

    • -0.214
    • Aliphatic Index

    • 34.76
    • Half Life

      • Mammalian:2.8 hour
      • Yeast:10 min
      • E.coli:2 min
    • Extinction Coefficient Cystines

    • 6335
    • Absorbance 280nm

    • 154.51
    • Polar Residues

    • 22

DRAMP02943

DRAMP02943 chydropathy plot
    • Function

    • Exhibits stronger antimicrobial activity against the Gram-positive bacterium S. aureus and fungi C. albicans and P. pastoris than Gram-negative bacterium E. coli. Binds to chitin (4.3 µM are required to obtain 50% of binding). Does not cause hemolysis on sheep erythrocytes. Has no blocking activity on the P-type calcium channel.
    • Tissue specificity

    • Granular hemocytes, small secretory granules.
    • Domain

    • The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
  • ·Literature 1
    • Title

    • Horseshoe crab hemocyte-derived antimicrobial polypeptides, tachystatins, with sequence similarity to spider neurotoxins.
    • Reference

    • J Biol Chem. 1999 Sep 10;274(37):26172-26178.
    • Author

    • Osaki T, Omotezako M, Nagayama R, Hirata M, Iwanaga S, Kasahara J, Hattori J, Ito I, Sugiyama H, Kawabata S.
  • ·Literature 2
    • Title

    • The solution structure of horseshoe crab antimicrobial peptide tachystatin B with an inhibitory cystine-knot motif.
    • Reference

    • J Pept Sci. 2007 Apr;13(4):269-279.
    • Author

    • Fujitani N, Kouno T, Nakahara T, Takaya K, Osaki T, Kawabata S, Mizuguchi M, Aizawa T, Demura M, Nishimura S, Kawano K.