Summary: Potassium-channel blocking toxin
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This is the Wikipedia entry entitled "Sea anemone neurotoxin". More...
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Sea anemone neurotoxin Edit Wikipedia article
Structure of the neurotoxin ATX Ia from Anemonia sulcata.
|SCOPe||1atx / SUPFAM|
|Antihypertensive protein BDS-I/II|
Structure of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata.
|SCOPe||2bds / SUPFAM|
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.
This family also includes the antihypertensive and antiviral proteins BDS-I ( ) and BDS-II ( ) 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. Both peptides are known to specifically block the Kv3.4 potassium channel, and thus bring about a decrease in blood pressure. Moreover, they inhibit the cytopathic effects of mouse hepatitis virus strain MHV-A59 on mouse liver cells, by an unknown mechanism.
- Widmer H, Billeter M, WÃ¼thrich K (1989). "Three-dimensional structure of the neurotoxin ATX Ia from Anemonia sulcata in aqueous solution determined by nuclear magnetic resonance spectroscopy". Proteins. 6 (4): 357â€“71. doi:10.1002/prot.340060403. PMID 2576133.
- Driscoll PC, Gronenborn AM, Beress L, Clore GM (March 1989). "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): 2188â€“98. doi:10.1021/bi00431a033. PMID 2566326.
- Norton TR (1981). "Cardiotonic polypeptides from Anthopleura xanthogrammica (Brandt) and A. elegantissima (Brandt)". Fed. Proc. 40 (1): 21â€“5. PMID 6108877.
- Yasunobu KT, Norton TR, Reimer NS, Yasunobu CL (1985). "Amino acid sequence of the Anthopleura xanthogrammica heart stimulant, anthopleurin-B". J. Biol. Chem. 260 (15): 8690â€“3. PMID 4019448.
- Scanlon MJ, Pallaghy PK, Norton RS, Monks SA (1995). "Solution structure of the cardiostimulant polypeptide anthopleurin-B and comparison with anthopleurin-A". Structure. 3 (8): 791â€“803. doi:10.1016/s0969-2126(01)00214-3. PMID 7582896.
- Clore GM, Driscoll PC, Gronenborn AM, Beress L (1989). "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): 2188â€“2198. doi:10.1021/bi00431a033. PMID 2566326.
- Lazdunski M, Schweitz H, Diochot S, Beress L (1998). "Sea anemone peptides with a specific blocking activity against the fast inactivating potassium channel Kv3.4". J. Biol. Chem. 273 (12): 6744â€“6749. doi:10.1074/jbc.273.12.6744. PMID 9506974.
- Schweitz, Hugues; Bruhn, Thomas; Guillemare, Eric; Moinier, Danielle; Lancelin, Jean-Marc; BÃ©ress, LÃ¡szlÃ³; 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): 25121â€“25126. doi:10.1074/jbc.270.42.25121. ISSN 0021-9258. PMID 7559645.
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Potassium-channel blocking toxin Provide feedback
This family features the antihypertensive and antiviral proteins BDS-I (P11494) and BDS-II (P59084) expressed by Anemonia sulcata. BDS-I is organised into a triple-stranded antiparallel beta-sheet, with an additional small antiparallel beta-sheet at the N-terminus . Both peptides are known to specifically block the Kv3.4 potassium channel, and thus bring about a decrease in blood pressure . Moreover, they inhibit the cytopathic effects of mouse hepatitis virus strain MHV-A59 on mouse liver cells, by an unknown mechanism .
Driscoll PC, Gronenborn AM, Beress L, Clore GM; , Biochemistry 1989;28:2188-2198.: 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. PUBMED:2566326 EPMC:2566326
Diochot S, Schweitz H, Beress L, Lazdunski M; , J Biol Chem 1998;273:6744-6749.: Sea anemone peptides with a specific blocking activity against the fast inactivating potassium channel Kv3.4. PUBMED:9506974 EPMC:9506974
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR012414
This entry represents the sea anemone type 3 (BDS) potassium channel toxins. Family members include toxin APETx1 and 2, and the antihypertensive and antiviral proteins BDS-I ( SWISSPROT ) and BDS-II ( SWISSPROT ) expressed by Anemonia sulcata. BDS-I is organised into a triple-stranded antiparallel beta-sheet, with an additional small antiparallel beta-sheet at the N terminus [ PUBMED:2566326 ]. The proteins are known to specifically block the Kv3.4 potassium channel, and thus bring about a decrease in blood pressure [ PUBMED:9506974 ]. Moreover, they inhibit the cytopathic effects of mouse hepatitis virus strain MHV-A59 on mouse liver cells, by an unknown mechanism [ PUBMED:2566326 ].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||nematocyst (GO:0042151)|
|Molecular function||ion channel inhibitor activity (GO:0008200)|
|toxin activity (GO:0090729)|
|Biological process||pathogenesis (GO:0009405)|
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This clan includes diverse defensins as well as myotoxins.
The clan contains the following 15 members:DEFB136 Defensin_1 Defensin_3 Defensin_4 Defensin_beta Defensin_beta_2 Defensin_big Defensin_int Defensin_RK-1 Inhibitor_I68 Laterosporulin Meleagrin Myotoxins Pelovaterin Toxin_4
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|Seed source:||Pfam-B_56105 (release 14.0)|
|Number in seed:||10|
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