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From Proteopedia
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== ECTATOMIN 1ECI == | == ECTATOMIN 1ECI == | ||
<StructureSection load='1eci' size='340' side='right' caption='1ECI<Structure load='' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | <StructureSection load='1eci' size='340' side='right' caption='1ECI<Structure load='' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | ||
| - | Ectatomin is a toxic component from Ectatomma tuberculatum ant venom. It contains two homologous polypeptide chains with 37 and 34 residues. The chains are linked together by a disulfide bond. Ectatomin in a cell leads to an irreversible increase in ion leakage, a decrease in membrane resistance, and eventually cell death. Ectatomin is found to be the most potent toxic peptide from ant venom because it blocks the calcium channel in the victims. | + | Ectatomin is a water soluble toxic component from Ectatomma tuberculatum ant venom. It contains two homologous polypeptide chains with 37 and 34 residues. The chains are linked together by a disulfide bond. Ectatomin in a cell leads to an irreversible increase in ion leakage, a decrease in membrane resistance, and eventually cell death. Ectatomin is found to be the most potent toxic peptide from ant venom because it blocks the calcium channel in the victims. |
== Structure == | == Structure == | ||
| - | + | <span> Ectatomin is a dimeric peptide connected by a disulfide bond. | |
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== Subunits == | == Subunits == | ||
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<span> Subunit B </span> | <span> Subunit B </span> | ||
| - | == | + | == Function == |
| + | <span> Ectatomin is a calcium channel blocker | ||
| + | pore-forming peptide cytotoxic | ||
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| + | == Spectroscopy == | ||
| + | <span> 1ECI produces 20 NMR structures. | ||
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Revision as of 15:32, 26 April 2017
Contents |
ECTATOMIN 1ECI
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Ectatomin is a water soluble toxic component from Ectatomma tuberculatum ant venom. It contains two homologous polypeptide chains with 37 and 34 residues. The chains are linked together by a disulfide bond. Ectatomin in a cell leads to an irreversible increase in ion leakage, a decrease in membrane resistance, and eventually cell death. Ectatomin is found to be the most potent toxic peptide from ant venom because it blocks the calcium channel in the victims.
Structure
Ectatomin is a dimeric peptide connected by a disulfide bond.
Subunits
Subunit B
Function
Ectatomin is a calcium channel blocker pore-forming peptide cytotoxic
Spectroscopy
1ECI produces 20 NMR structures.
References
Pluzhnikov, Kirill, et al. “Analysis of Ectatomin Action on Cell Membranes.” European Journal of Biochemistry 262.2 (1999):501. Academic Search Complete. Web. 13 Feb. 2017
Touchard, Axel, Samira R. Aili, Eduardo G. Fox, Pierre Escoubas, Jerome Orivel, Graham M. Nicholson, and Alain Dejuan. “The Biochemical Toxin Arsenal from Ant Venoms.” MDPI. N.p., 20 Jan. 2016. Web. 13 Feb. 2017.
