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| This family also includes the ] and ] proteins 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= |
This family also includes the ] and ] proteins 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" />. | ||
| ==References== | ==References== | ||
Revision as of 10:13, 11 June 2008
Protein family| Anenome neurotoxin | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||||
| Symbol | Toxin_4 | ||||||||||
| Pfam | PF00706 | ||||||||||
| InterPro | IPR000693 | ||||||||||
| SCOP2 | 1atx / SCOPe / SUPFAM | ||||||||||
| OPM superfamily | 56 | ||||||||||
| OPM protein | 1apf | ||||||||||
| |||||||||||
| Antihypertensive protein BDS-I/II | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||||
| Symbol | BDS_I_II | ||||||||||
| Pfam | PF07936 | ||||||||||
| InterPro | IPR012414 | ||||||||||
| SCOP2 | 2bds / SCOPe / SUPFAM | ||||||||||
| OPM superfamily | 56 | ||||||||||
| OPM protein | 1bds | ||||||||||
| |||||||||||
Sea 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 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 (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.
References
- Norton TR (1981). "Cardiotonic polypeptides from Anthopleura xanthogrammica (Brandt) and A. elegantissima (Brandt)". Fed. Proc. 40 (1): -. 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): -. PMID 4019448.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - 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): -. PMID 7582896.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ 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.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - 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.
{{cite journal}}: CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link)
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