Summary: Anenome neurotoxin
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.
|Antihypertensive protein BDS-I/II|
Structure of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata.
Sea anemone neurotoxin is the name given to neurotoxins produced by sea anemones with related structure and function. A number of proteins belong to this 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 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, Wüthrich 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): 357–71. 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): 2188–98. doi:10.1021/bi00431a033. PMID 2566326.
- Norton TR (1981). "Cardiotonic polypeptides from Anthopleura xanthogrammica (Brandt) and A. elegantissima (Brandt)". Fed. Proc. 40 (1): 21–5. 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): 8690–3. 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): 791–803. 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): 2188–2198. 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): 6744–6749. doi:10.1074/jbc.273.12.6744. PMID 9506974.
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Anenome neurotoxin Provide feedback
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External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR000693Sea anemones produce many different neurotoxins with related structure and function. Proteins belonging to this family include the neurotoxins, of which there are several, 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 prearations of crustaceans, where it increases transmitter release, causing firing of the axons. Three disulphide bonds are present in this protein [PUBMED:6108877, PUBMED:4019448, PUBMED:7582896].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||extracellular region (GO:0005576)|
|Biological process||regulation of signal transduction (GO:0009966)|
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|Seed source:||Pfam-B_589 (release 2.1)|
|Number in seed:||7|
|Number in full:||75|
|Average length of the domain:||43.60 aa|
|Average identity of full alignment:||56 %|
|Average coverage of the sequence by the domain:||70.66 %|
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build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||12|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Toxin_4 domain has been found. There are 7 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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