Sea anemone neurotoxin

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Anemone neurotoxin
PDB 1atx EBI.jpg
Structure of the neurotoxin ATX Ia from Anemonia sulcata.[1]
Identifiers
Symbol Toxin_4
Pfam PF00706
Pfam clan CL0075
InterPro IPR000693
SCOP 1atx
SUPERFAMILY 1atx
OPM superfamily 56
OPM protein 1apf
Antihypertensive protein BDS-I/II
PDB 1bds EBI.jpg
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
SCOP 2bds
SUPERFAMILY 2bds
OPM superfamily 56
OPM protein 1bds

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.[3][4][5]

This family also includes 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.[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]

See also[edit]

References[edit]

  1. ^ 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. 
  2. ^ 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. 
  3. ^ Norton TR (1981). "Cardiotonic polypeptides from Anthopleura xanthogrammica (Brandt) and A. elegantissima (Brandt)". Fed. Proc. 40 (1): 21–5. PMID 6108877. 
  4. ^ 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. 
  5. ^ 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. PMID 7582896. 
  6. ^ a b 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. 
  7. ^ 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. 

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