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'''Sea anemone neurotoxin''' is the name given to ]s produced by ]s with related structure and function. |
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'''Sea anemone neurotoxin''' is the name given to ]s produced by ]s with related structure and function. |
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A number of proteins belong to this family, including ''calitoxin'' and ''anthopleurin''. The neurotoxins bind specifically to the ], 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 ]s, where it increases transmitter release, causing firing of the ]s. Three disulfide bonds are present in this protein.<ref name="PUB00034660">{{cite journal |author=Norton TR |title=Cardiotonic polypeptides from Anthopleura xanthogrammica (Brandt) and A. elegantissima (Brandt) |journal=Fed. Proc. |volume=40 |issue=1 |pages=21–5 |year=1981 |pmid=6108877}}</ref><ref name="PUB00034661">{{cite journal |author=Yasunobu KT, Norton TR, Reimer NS, Yasunobu CL |title=Amino acid sequence of the Anthopleura xanthogrammica heart stimulant, anthopleurin-B |journal=J. Biol. Chem. |volume=260 |issue=15 |pages=8690–3 |year=1985 |pmid=4019448}}</ref><ref name="PUB00023402">{{cite journal |author=Scanlon MJ, Pallaghy PK, Norton RS, Monks SA |title=Solution structure of the cardiostimulant polypeptide anthopleurin-B and comparison with anthopleurin-A |journal=Structure |volume=3 |issue=8 |pages=791–803 |year=1995 |pmid=7582896}}</ref> |
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A number of proteins belong to this family, including ''calitoxin'' and ''anthopleurin''. The neurotoxins bind specifically to the ], 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 ]s, where it increases transmitter release, causing firing of the ]s. Three disulfide bonds are present in this protein.<ref name="PUB00034660">{{cite journal |author=Norton TR |title=Cardiotonic polypeptides from Anthopleura xanthogrammica (Brandt) and A. elegantissima (Brandt) |journal=Fed. Proc. |volume=40 |issue=1 |pages=21–5 |year=1981 |pmid=6108877}}</ref><ref name="PUB00034661">{{cite journal |author=Yasunobu KT, Norton TR, Reimer NS, Yasunobu CL |title=Amino acid sequence of the Anthopleura xanthogrammica heart stimulant, anthopleurin-B |journal=J. Biol. Chem. |volume=260 |issue=15 |pages=8690–3 |year=1985 |pmid=4019448}}</ref><ref name="PUB00023402">{{cite journal |author=Scanlon MJ, Pallaghy PK, Norton RS, Monks SA |title=Solution structure of the cardiostimulant polypeptide anthopleurin-B and comparison with anthopleurin-A |journal=Structure |volume=3 |issue=8 |pages=791–803 |year=1995 |pmid=7582896 |doi=10.1016/s0969-2126(01)00214-3}}</ref> |
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This family also includes the ] and ]s BDS-I ({{Uniprot|P11494}}) and BDS-II ({{Uniprot|P59084}}) expressed by '']''. BDS-I is organised into a triple-stranded antiparallel beta-sheet, with an additional small antiparallel beta-sheet at the N-terminus.<ref name="PUB00016458">{{cite journal |author=Clore GM, Driscoll PC, Gronenborn AM, Beress L |title=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 |journal=Biochemistry |volume=28 |issue=5 |pages=2188–2198 |year=1989 |pmid=2566326 |doi=10.1021/bi00431a033}}</ref> Both peptides are known to specifically block the Kv3.4 potassium channel, and thus bring about a decrease in blood pressure.<ref name="PUB00016411">{{cite journal |author=Lazdunski M, Schweitz H, Diochot S, Beress L |title=Sea anemone peptides with a specific blocking activity against the fast inactivating potassium channel Kv3.4 |journal=J. Biol. Chem. |volume=273 |issue=12 |pages=6744–6749 |year=1998 |pmid=9506974 |doi=10.1074/jbc.273.12.6744}}</ref> Moreover, they inhibit the cytopathic effects of mouse hepatitis virus strain MHV-A59 on mouse liver cells, by an unknown mechanism.<ref name="PUB00016458"/> |
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This family also includes the ] and ]s BDS-I ({{Uniprot|P11494}}) and BDS-II ({{Uniprot|P59084}}) expressed by '']''. BDS-I is organised into a triple-stranded antiparallel beta-sheet, with an additional small antiparallel beta-sheet at the N-terminus.<ref name="PUB00016458">{{cite journal |author=Clore GM, Driscoll PC, Gronenborn AM, Beress L |title=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 |journal=Biochemistry |volume=28 |issue=5 |pages=2188–2198 |year=1989 |pmid=2566326 |doi=10.1021/bi00431a033}}</ref> Both peptides are known to specifically block the Kv3.4 potassium channel, and thus bring about a decrease in blood pressure.<ref name="PUB00016411">{{cite journal |author=Lazdunski M, Schweitz H, Diochot S, Beress L |title=Sea anemone peptides with a specific blocking activity against the fast inactivating potassium channel Kv3.4 |journal=J. Biol. Chem. |volume=273 |issue=12 |pages=6744–6749 |year=1998 |pmid=9506974 |doi=10.1074/jbc.273.12.6744}}</ref> Moreover, they inhibit the cytopathic effects of mouse hepatitis virus strain MHV-A59 on mouse liver cells, by an unknown mechanism.<ref name="PUB00016458"/> |
Structure of the neurotoxin ATX Ia from Anemonia sulcata.
Structure of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata.