General Information of This Peptide
Peptide ID
BTDP008377
Peptide Name
Kappa-actitoxin-Bgr1a
Symonym
Potassium channel toxin Bgk
Species
Bunodosoma granuliferum (Red warty sea anemone)
Uniprot Name
K1B_BUNGR
Alphafold ID
P29186
3D Structure
Download
2D Sequence
3D Structure
Source
RSCB PDB: 1BGK
Sequence
VCRDWFKETACRHAKSLGNCRTSQKYRANCAKTCELC
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Sequence Length
37
Mass (Da)
4282
Sequence Removed Signal Peptide
VCRDWFKETACRHAKSLGNCRTSQKYRANCAKTCELC
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Disulfide Bond
2-37;11-30;20-34
PDB ID
1BGK
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Kingdom: Metazoa
Phylum: Cnidaria
Class: Anthozoa
Order: Actiniaria
Family: Actiniidae
Genus: Bunodosoma
Species: Bunodosoma granuliferum
Full List of Activity Data of This Peptide Toxin
                        Target Name Activity Data Type Activity Data Concentration Note Reference
 Target Info    Kv1.1 Dissociation constant
6 nM
.
Blocker
[1- 8]
 Target Info    Kv1.1 Dissociation constant
6 nM
.
Blocker
[2]
 Target Info    Kv1.3 Dissociation constant
10 nM
.
Blocker
[2]
 Target Info    Kv1.3 Dissociation constant
10 - 39 nM
.
Blocker
[1- 8]
 Target Info    Kv1.2 Dissociation constant
15 nM
.
Blocker
[1- 8]
 Target Info    Kv1.2 Dissociation constant
15 nM
.
Blocker
[2]
 Target Info    Kv1.1 Dissociation constant
17 nM
.
Blocker
[9]
 Target Info    KCa3.1 Dissociation constant
172 nM
.
Blocker
[3]
 Target Info    KCa3.1 Dissociation constant
172 nM
.
Blocker
[1- 8]
 Target Info    Kv1.6 Inhibition constant
0.013 nM
.
Blocker
[5]
 Target Info    Kv1.1 Inhibition constant
0.034 nM
.
Blocker
[5]
 Target Info    Kv1.2 Inhibition constant
0.066 nM
.
Blocker
[5]
 Target Info    Kv1.3 Inhibition constant
0.777 nM
.
Blocker
[5]
 Target Info    Kv1.2-1.1 Inhibition constant
8 nM
.
Blocker
[5]
 Target Info    Kv3.1 Inhibition rate .
125 nM
Blocker
[2]
 Target Info    Kv3.1 Inhibition rate .
125 nM
Blocker
[1- 8]
 Target Info    Kv1 IC50
3.6 nM
.
Blocker
[1- 8]
References
Ref 1 A potassium channel toxin from the secretion of the sea anemone Bunodosoma granulifera. Isolation, amino acid sequence and biological activity. Biochim Biophys Acta. 1993 May 7;1157(1):86-92. doi: 10.1016/0304-4165(93)90082-j.
Ref 2 A potassium-channel toxin from the sea anemone Bunodosoma granulifera, an inhibitor for Kv1 channels. Revision of the amino acid sequence, disulfide-bridge assignment, chemical synthesis, and biological activity. Eur J Biochem. 1997 Feb 15;244(1):192-202. doi: 10.1111/j.1432-1033.1997.00192.x.
Ref 3 Structural conservation of the pores of calcium-activated and voltage-gated potassium channels determined by a sea anemone toxin. J Biol Chem. 1999 Jul 30;274(31):21885-92. doi: 10.1074/jbc.274.31.21885.
Ref 4 Mapping the functional anatomy of BgK on Kv1.1, Kv1.2, and Kv1.3. Clues to design analogs with enhanced selectivity. J Biol Chem. 1999 Dec 10;274(50):35653-61. doi: 10.1074/jbc.274.50.35653.
Ref 5 Characterization of a novel radiolabeled peptide selective for a subpopulation of voltage-gated potassium channels in mammalian brain. J Biol Chem. 2002 Feb 8;277(6):3886-93. doi: 10.1074/jbc.M109886200. Epub 2001 Nov 13.
Ref 6 Peptide fingerprinting of the neurotoxic fractions isolated from the secretions of sea anemones Stichodactyla helianthus and Bunodosoma granulifera. New members of the APETx-like family identified by a 454 pyrosequencing approach. Peptides. 2012 Mar;34(1):26-38. doi: 10.1016/j.peptides.2011.10.011. Epub 2011 Oct 12.
Ref 7 Development of a rational nomenclature for naming peptide and protein toxins from sea anemones. Toxicon. 2012 Sep 15;60(4):539-50. doi: 10.1016/j.toxicon.2012.05.020. Epub 2012 Jun 5.
Ref 8 On the convergent evolution of animal toxins. Conservation of a diad of functional residues in potassium channel-blocking toxins with unrelated structures. J Biol Chem. 1997 Feb 14;272(7):4302-9. doi: 10.1074/jbc.272.7.4302.
Ref 9 Structure of the BgK-Kv1.1 complex based on distance restraints identified by double mutant cycles. Molecular basis for convergent evolution of Kv1 channel blockers. J Biol Chem. 2002 Oct 4;277(40):37406-13. doi: 10.1074/jbc.M206205200. Epub 2002 Jul 19.
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