General Information
-
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
Activity Information
-
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
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
- 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
- 1BAH-> 2CRD-> 
-
Predicted Structure
- There is no predicted structure for DRAMP03755.
Physicochemical Information
-
Formula
- C176H286N58O55S7
Absent Amino Acids
- ADIP
Common Amino Acids
- C
Mass
- 4318.98
PI
- 9.34
Basic Residues
- 8
Acidic Residues
- 1
Hydrophobic Residues
- 5
Net Charge
- +7
-
Boman Index
- -107.57
Hydrophobicity
- -0.832
Aliphatic Index
- 26.22
Half Life
-
- Mammalian:0.8 hour
- Yeast:10 min
- E.coli:>10 hour
Extinction Coefficient Cystines
- 7365
Absorbance 280nm
- 204.58
Polar Residues
- 20
DRAMP03755
Comments Information
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 Information
- ·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.