Sea anemone neurotoxin

Anemone neurotoxin

Structure of the neurotoxin ATX Ia from Anemonia sulcata.[1]

Identifiers
Symbol| Toxin_4
Pfam| PF00706
Pfam clan| CL0075
InterPro| IPR000693
SCOP2| 1atx / SCOPe / SUPFAM
OPM superfamily| 54
OPM protein| 1apf
| Available protein structures:

Pfam | structures / ECOD
PDB| RCSB PDB; PDBe; PDBj
PDBsum| structure summary
Antihypertensive protein BDS-I/II

Structure of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata.[2]

Identifiers
Symbol| BDS_I_II
Pfam| PF07936
Pfam clan| CL0075
InterPro| IPR012414
SCOP2| 2bds / SCOPe / SUPFAM
OPM superfamily| 54
OPM protein| 1bds
| Available protein structures:

Pfam | structures / ECOD
PDB| RCSB PDB; PDBe; PDBj
PDBsum| structure summary

Sea anemone neurotoxin is the name given to neurotoxins produced by sea anemones with related structure and function. Sea anemone neurotoxins can be divided in two functional groups that either specifically target the sodium channel or the potassium channel.

A number of proteins belong to the sodium channel toxin family, including calitoxin and anthopleurin. The neurotoxins bind specifically to the sodium channel, thereby delaying its inactivation during signal transduction, resulting in strong stimulation of mammalian cardiac muscle contraction. Calitoxin 1 has been found in neuromuscular preparations of crustaceans, where it increases transmitter release, causing firing of the axons. Three disulfide bonds are present in this protein.[3][4][5]

This family also includes the antihypertensive and antiviral proteins BDS-I (P11494) and BDS-II (P59084) expressed by Anemonia viridis (previously Anemonia sulcata). BDS-I is organised into a triple-stranded antiparallel beta-sheet, with an additional small antiparallel beta-sheet at the N-terminus.[6] Both peptides are known to specifically block the Kv3.4 potassium channel, and thus bring about a decrease in blood pressure.[7] Moreover, they inhibit the cytopathic effects of mouse hepatitis virus strain MHV-A59 on mouse liver cells, by an unknown mechanism.[6]

The potassium channel toxin family include kaliseptine and kalicludines,[8] and was also isolated from Anemonia viridis.

## See also

* AETX
* Halcurin
* Cangitoxin

## References

1. ↑ "Three-dimensional structure of the neurotoxin ATX Ia from Anemonia sulcata in aqueous solution determined by nuclear magnetic resonance spectroscopy". Proteins 6 (4): 357–71. 1989. doi:10.1002/prot.340060403. PMID 2576133.
2. ↑ "Determination of the three-dimensional solution structure of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata: a study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing". Biochemistry 28 (5): 2188–98. March 1989. doi:10.1021/bi00431a033. PMID 2566326.
3. ↑ Norton TR (1981). "Cardiotonic polypeptides from Anthopleura xanthogrammica (Brandt) and A. elegantissima (Brandt)". Fed. Proc. 40 (1): 21–5. PMID 6108877.
4. ↑ "Amino acid sequence of the Anthopleura xanthogrammica heart stimulant, anthopleurin-B". J. Biol. Chem. 260 (15): 8690–3. 1985. doi:10.1016/S0021-9258(17)39403-6. PMID 4019448.
5. ↑ "Solution structure of the cardiostimulant polypeptide anthopleurin-B and comparison with anthopleurin-A". Structure 3 (8): 791–803. 1995. doi:10.1016/s0969-2126(01)00214-3. PMID 7582896.
6. ↑ 6.0 6.1 "Determination of the three-dimensional solution structure of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata: a study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing". Biochemistry 28 (5): 2188–2198. 1989. doi:10.1021/bi00431a033. PMID 2566326.
7. ↑ "Sea anemone peptides with a specific blocking activity against the fast inactivating potassium channel Kv3.4". J. Biol. Chem. 273 (12): 6744–6749. 1998. doi:10.1074/jbc.273.12.6744. PMID 9506974.
8. ↑ Schweitz, Hugues; Bruhn, Thomas; Guillemare, Eric; Moinier, Danielle; Lancelin, Jean-Marc; Béress, László; Lazdunski, Michel (1995-10-20). "Kalicludines and Kaliseptine TWO DIFFERENT CLASSES OF SEA ANEMONE TOXINS FOR VOLTAGE-SENSITIVE K+ CHANNELS". Journal of Biological Chemistry 270 (42): 25121–25126. doi:10.1074/jbc.270.42.25121. ISSN 0021-9258. PMID 7559645. http://www.jbc.org/content/270/42/25121.

This article incorporates text from the public domain Pfam and InterPro: IPR000693

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