AMPDB_156 | Potassium channel toxin alpha-KTx 1.1
PEPTIDE SUMMARY
Potassium channel toxin alpha-KTx 1.1
1 General Description
AMPDB ID: AMPDB_156
Protein Names: Potassium channel toxin alpha-KTx 1.1 (ChTX-Lq1) (ChTx-a) (Charybdotoxin) (CTX) (ChTX)
Protein Family: Short scorpion toxin superfamily; Potassium channel inhibitor family; Alpha-KTx 01 subfamily
Gene Name: Nil
Protein Length: 59 AA
Protein Existence: Evidence at protein level
2 Protein Sequence & Composition
2.1 Sequence
MKILSVLLLALIICSIVGWSEAQFTNVSCTTSKECWSVCQRLHNTSRGKCMNKKCRCYS
FASTA format
2.2 Composition
Counts of Amino Acids
'A': 2, 'R': 3, 'N': 3, 'D': 0, 'C': 7, 'Q': 2, 'E': 2, 'G': 2, 'H': 1, 'I': 4, 'L': 6, 'K': 5, 'M': 2, 'F': 1, 'P': 0, 'S': 8, 'T': 4, 'W': 2, 'Y': 1, 'V': 4
Frequencies of Amino Acids
'A': 3.39%, 'R': 5.08%, 'N': 5.08%, 'D': 0%, 'C': 11.86%, 'Q': 3.39%, 'E': 3.39%, 'G': 3.39%, 'H': 1.69%, 'I': 6.78%, 'L': 10.17%, 'K': 8.47%, 'M': 3.39%, 'F': 1.69%, 'P': 0%, 'S': 13.56%, 'T': 6.78%, 'W': 3.39%, 'Y': 1.69%, 'V': 6.78%
Missing Amino Acid(s)
D, P
Most Occurring Amino Acid(s)
S
Less Occurring Amino Acid(s)
F, H, Y
Hydrophobic Amino Acid(s) Count
23
Hydrophilic Amino Acid(s) Count
36
Basic Amino Acid(s) Count
2
Acidic Amino Acid(s) Count
9
Modified Amino Acid(s) Count
0
Modified Amino Acid(s) Frequencies
0
Computed by biopython (version 1.79) & proteinAnalysis (version 1)
3 Physicochemical Properties
Sl. No. Properties Values Reference
1. Molecular Mass 6673.96 Da Computed by ProtParam module (biopython 1.79)
2. Aliphatic Index 89.153 Computed by ProtParam module (biopython 1.79)
3. Instability Index (Half Life) 44.042 Computed by ProtParam module (biopython 1.79)
4. Hydrophobicity (GRAVY) 0.195 Computed by ProtParam module (biopython 1.79)
5. Hydrophobic Moment 0.544 Computed by ProtParam module (biopython 1.79)
6. Isoelectric Point 8.952 Computed by ProtParam module (biopython 1.79)
7. Charge (at pH 7) 5.656 Computed by ProtParam module (biopython 1.79)
8. Secondary Structure Fraction 0.305, 0.22, 0.203 [Helix, Turn, Sheet] Computed by ProtParam module (biopython 1.79)
9. Aromaticity 0.068 Computed by ProtParam module (biopython 1.79)
10. Molar Extinction Coefficient (cysteine|cystine) 12490, 12865 Computed by ProtParam module (biopython 1.79)
4 Activity Details
4.1 Target Organism(s)
B.subtilis (Gram-positive), C.albicans, E.coli (Gram-negative), S.aureus (Gram-positive)
4.2 Antimicrobial Activity
Antibiotic, Antimicrobial, Fungicide, Anti-candida, Anti-gram-negative, Anti-gram-Positive
4.3 Enzymatic Activity
Not found
4.4 Inhibitory Effect
Not found
4.5 Other Biological Activity
Toxin, Non-hemolytic, Non-ribosomal
Activity data manually curated from Literature and UniProt
5 Database Cross-references
5.1 Literature Database
5.1.1 PubMed
Citation 1: Froy O, Sagiv T, Poreh M, et al. Dynamic diversification from a putative common ancestor of scorpion toxins affecting sodium, potassium, and chloride channels. J Mol Evol. 1999;48(2):187-96. Published 1999 Feb. doi:10.1007/pl00006457
PMID: 9929387
Citation 2: Gimenez-Gallego G, Navia MA, Reuben JP, et al. Purification, sequence, and model structure of charybdotoxin, a potent selective inhibitor of calcium-activated potassium channels. Proc Natl Acad Sci U S A. 1988;85(10):3329-33. Published 1988 May. doi:10.1073/pnas.85.10.3329
PMID: 2453055
Citation 3: Schweitz H, Bidard JN, Maes P, et al. Charybdotoxin is a new member of the K+ channel toxin family that includes dendrotoxin I and mast cell degranulating peptide. Biochemistry. 1989;28(25):9708-14. Published 1989 Dec 12. doi:10.1021/bi00451a025
PMID: 2482078
Citation 4: Lucchesi K, Ravindran A, Young H, et al. Analysis of the blocking activity of charybdotoxin homologs and iodinated derivatives against Ca2+-activated K+ channels. J Membr Biol. 1989;109(3):269-81. Published 1989 Aug. doi:10.1007/BF01870284
PMID: 2477548
Citation 5: Lambert P, Kuroda H, Chino N, et al. Solution synthesis of charybdotoxin (ChTX), a K+ channel blocker. Biochem Biophys Res Commun. 1990;170(2):684-90. Published 1990 Jul 31. doi:10.1016/0006-291x(90)92145-p
PMID: 1696475
Citation 6: Sugg EE, Garcia ML, Reuben JP, et al. Synthesis and structural characterization of charybdotoxin, a potent peptidyl inhibitor of the high conductance Ca2(+)-activated K+ channel. J Biol Chem. 1990;265(31):18745-8. Published 1990 Nov 5. doi:
PMID: 1699936
Citation 7: Garcia ML, Garcia-Calvo M, Hidalgo P, et al. Purification and characterization of three inhibitors of voltage-dependent K+ channels from Leiurus quinquestriatus var. hebraeus venom. Biochemistry. 1994;33(22):6834-9. Published 1994 Jun 7. doi:10.1021/bi00188a012
PMID: 8204618
Citation 8: Grissmer S, Nguyen AN, Aiyar J, et al. Pharmacological characterization of five cloned voltage-gated K+ channels, types Kv1.1, 1.2, 1.3, 1.5, and 3.1, stably expressed in mammalian cell lines. Mol Pharmacol. 1994;45(6):1227-34. Published 1994 Jun. doi:
PMID: 7517498
Citation 9: Zhang M, Korolkova YV, Liu J, et al. BeKm-1 is a HERG-specific toxin that shares the structure with ChTx but the mechanism of action with ErgTx1. Biophys J. 2003;84(5):3022-36. Published 2003 May. doi:10.1016/S0006-3495(03)70028-9
PMID: 12719233
Citation 10: Castle NA, London DO, Creech C, et al. Maurotoxin: a potent inhibitor of intermediate conductance Ca2+-activated potassium channels. Mol Pharmacol. 2003;63(2):409-18. Published 2003 Feb. doi:10.1124/mol.63.2.409
PMID: 12527813
Citation 11: Yount NY, Yeaman MR, Yeaman MR. Multidimensional signatures in antimicrobial peptides. Proc Natl Acad Sci U S A. 2004;101(19):7363-8. Published 2004 May 11. doi:10.1073/pnas.0401567101
PMID: 15118082
Citation 12: Takacs Z, Toups M, Kollewe A, et al. A designer ligand specific for Kv1.3 channels from a scorpion neurotoxin-based library. Proc Natl Acad Sci U S A. 2009;106(52):22211-6. Published 2009 Dec 29. doi:10.1073/pnas.0910123106
PMID: 20007782
Citation 13: Meng L, Xie Z, Zhang Q, et al. Scorpion Potassium Channel-blocking Defensin Highlights a Functional Link with Neurotoxin. J Biol Chem. 2016;291(13):7097-106. Published 2016 Mar 25. doi:10.1074/jbc.M115.680611
PMID: 26817841
Citation 14: Kasheverov IE, Oparin PB, Zhmak MN, et al. Scorpion toxins interact with nicotinic acetylcholine receptors. FEBS Lett. 2019;593(19):2779-2789. Published 2019 Oct. doi:10.1002/1873-3468.13530
PMID: 31276191
Citation 15: Massefski W Jr, Redfield AG, Hare DR, et al. Molecular structure of charybdotoxin, a pore-directed inhibitor of potassium ion channels. Science. 1990;249(4968):521-4. Published 1990 Aug 3. doi:10.1126/science.1696395
PMID: 1696395
Citation 16: Massefski W Jr, Redfield AG, Hare DR, et al. Molecular structure of charybdotoxin: retraction. Science. 1991;252(5006):631. Published 1991 May 3. doi:10.1126/science.252.5006.631.b
PMID: 2024115
Citation 17: Bontems F, Roumestand C, Boyot P, et al. Three-dimensional structure of natural charybdotoxin in aqueous solution by 1H-NMR. Charybdotoxin possesses a structural motif found in other scorpion toxins. Eur J Biochem. 1991;196(1):19-28. Published 1991 Feb 26. doi:10.1111/j.1432-1033.1991.tb15780.x
PMID: 1705886
Citation 18: Bontems F, Roumestand C, Gilquin B, et al. Refined structure of charybdotoxin: common motifs in scorpion toxins and insect defensins. Science. 1991;254(5037):1521-3. Published 1991 Dec 6. doi:10.1126/science.1720574
PMID: 1720574
Citation 19: Bontems F, Gilquin B, Roumestand C, et al. Analysis of side-chain organization on a refined model of charybdotoxin: structural and functional implications. Biochemistry. 1992;31(34):7756-64. Published 1992 Sep 1. doi:10.1021/bi00149a003
PMID: 1380828
Citation 20: Bonmatin JM, Genest M, Petit MC, et al. Progress in multidimensional NMR investigations of peptide and protein 3-D structures in solution. From structure to functional aspects. Biochimie. 1992;74(9-10):825-36. Published 1992 Sep-Oct. doi:10.1016/0300-9084(92)90065-m
PMID: 1467342
Citation 21: Song J, Gilquin B, Jamin N, et al. 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. Biochemistry. 1997;36(13):3760-6. Published 1997 Apr 1. doi:10.1021/bi962720h
PMID: 9092804
5.2 Protein Sequence Databases
UniProt: P13487
5.3 3D Structure Databases
Sl. no. PDB ID Method Resolution Access Links 3D View
AlphaFoldDB: P13487
5.4 Nucleotide Sequence Databases
No entries found in GenBank or EMBL
CCDS: Not found
RefSeq: Not found
5.5 Protein-Protein Interaction Databases
STRING: Not found
IntAct: Not found
MINT: Not found
DIP: Not found
BioGRID: Not found
5.6 Ligand Databases
BindingDB: Not found
DrugBank: Not found
ChEMBL: Not found
5.7 Family & Domain Databases
InterPro: IPR036574, IPR001947
PANTHER: Not found
PROSITE: PS01138
5.8 Genome Annotation Databases
Ensembl: Not found
KEGG: Not found
5.9 Phylogenomic Databases
GeneTree: Not found
5.10 Enzyme & Pathway Databases
BRENDA: Not found
BioCyc: Not found
5.11 Protein-RNA Interaction Databases
RNAct: Not found




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