Sandbox Reserved 1228
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
| - | zzz<Structure load='1ECI' size='350' frame='true' align='right' caption='Insert caption here' scene=' | + | zzz<Structure load='1ECI' size='350' frame='true' align='right' caption='Insert caption here' scene='Disulfide bonds 1' /> |
</StructureSection> | </StructureSection> | ||
Revision as of 21:03, 8 March 2017
Contents |
ECTATOMIN 1ECI
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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.
Structure
Function
Disease
Relevance
Structural highlights
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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.
