• • DRAMP ID

  • DRAMP03755

• • Peptide Name

  • Potassium channel toxin alpha-KTx 1.1 (ChTX-Lq1; charybdotoxin; Arthropods, animals)

• • Source

  • Leiurus quinquestriatus hebraeus (Yellow scorpion)

• • Family

  • Not found

• • Gene

  • Not found

• • Sequence

  • QFTNVSCTTSKECWSVCQRLHNTSRGKCMNKKCRCYS

• • Sequence Length

  • 37

• • UniProt Entry

  • P13487

• • Protein Existence

  • Protein level

• • Biological Activity

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

• • Target Organism

  • • Gram-positive bacteria: B.subtilis, S.aureus;
    • Gram-negative bacterium: E.coli.
    • Yeast: Candida albicans.

• • 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

  • Combine helix and strand structure

• • Structure Description

  • These structures show that charybdotoxin is composed of a beta-sheet linked to an alpha-helix by two disulphide bridges and to an extended fragment by the third disulphide bridge.

• • Helical Wheel Diagram

  • 

• • PDB ID

  • 1BAH,2CRD resolved by NMR.

• Predicted Structure

• There is no predicted structure for DRAMP03755.

DRAMP03755

• • Function

  • Potent selective inhibitor of high conductance (maxi-K), different medium and small conductance calcium-activated potassium channels (KCa/KCNM), as well as a voltage-dependent potassium channel (Kv1.3/KCNA3). It appears to block channel activity by a simple bimolecular inhibition process.

• • Tissue specificity

  • Expressed by the venom gland.

• • Domain

  • Has the structural arrangement of an alpha-helix connected to a beta-sheet by disulfide bonds (CSalpha/beta).

• • PTM

  • Contains three disulfide bonds.

• ·Literature 1

• • Title

  • Multidimensional signatures in antimicrobial peptides.

• • Pubmed ID

  • 15118082

• • Reference

  • Proc Natl Acad Sci U S A. 2004 May 11;101(19):7363-7368.

• • Author

  • Yount NY, Yeaman MR.

• ·Literature 2

• • Title

  • Three-dimensional structure of natural charybdotoxin in aqueous solution by 1H-NMR. Charybdotoxin possesses a structural motif found in other scorpion toxins.

• • Pubmed ID

  • 1705886

• • Reference

  • Eur J Biochem. 1991 Feb 26;196(1):19-28.

• • Author

  • Bontems F, Roumestand C, Boyot P, Gilquin B, Doljansky Y, Menez A, Toma F.

• ·Literature 3

• • Title

  • NMR solution structure of a two-disulfide derivative of charybdotoxin: structural evidence for conservation of scorpion toxin alpha/beta motif and its hydrophobic side chain packing.

• • Pubmed ID

  • 9092804

• • Reference

  • Biochemistry. 1997 Apr 1;36(13):3760-3766.

• • Author

  • Song J, Gilquin B, Jamin N, Drakopoulou E, Guenneugues M, Dauplais M, Vita C, Ménez A.

• ·Literature 4

• • Title

  • Analysis of side-chain organization on a refined model of charybdotoxin: structural and functional i

• • Pubmed ID

  • 1380828

• • Reference

  • Biochemistry. 1992 Sep 1;31(34):7756-7764.

• • Author

  • Bontems F, Gilquin B, Roumestand C, Ménez A, Toma F.