Sandbox Reserved 996: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='1eci' size='340' side='right' caption='[[1eci]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='1eci' size='340' side='right' caption='[[1eci]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
Ectatomin (1eci) is the main component of venom of the ant [https://en.wikipedia.org/wiki/Ectatomma_tuberculatum Ectatomma tuberculatum], making up 15%-18% of the crude venom and accounting for 90% of the venom's toxicity.<ref name="refthree" /> When bitten by E. tuberculatum, Ectatomin inserts into the target's [https://en.wikipedia.org/wiki/Cell_membrane cell membranes] and forms a nonselective [https://en.wikipedia.org/wiki/Ion_channel cation channel].<ref name="reftwo">PMID: 10336635</ref> The calculated [https://en.wikipedia.org/wiki/Isoelectric_point isoelectric point] and [https://en.wikipedia.org/wiki/Molecular_mass molecular weight] are 9.95 and 7928 Da, respectively.<ref name="refthree">PMID: 8033986</ref> | Ectatomin (1eci) is the main component of venom of the ant [https://en.wikipedia.org/wiki/Ectatomma_tuberculatum Ectatomma tuberculatum], making up 15%-18% of the crude venom and accounting for 90% of the venom's toxicity.<ref name="refthree" /> When bitten by E. tuberculatum, Ectatomin inserts into the target's [https://en.wikipedia.org/wiki/Cell_membrane cell membranes] and forms a nonselective [https://en.wikipedia.org/wiki/Ion_channel cation channel].<ref name="reftwo">PMID: 10336635</ref> The calculated [https://en.wikipedia.org/wiki/Isoelectric_point isoelectric point] and [https://en.wikipedia.org/wiki/Molecular_mass molecular weight] of Ectatomin are 9.95 and 7928 Da, respectively.<ref name="refthree">PMID: 8033986</ref> | ||
| Line 30: | Line 30: | ||
For the second and third proposed mechanisms of action, Ectatomin has also been shown to inhibit kinases, specifically protein tyrosine kinase and protein kinase C, and Ca2+ channels. Kinase inhibition would potentially allow Ectatomin to interfere with various components of signal transduction. Calcium channel inhibition would potentially allow Ectatomin to affect physiological processes such as contraction, neurotransmitter release and neuronal activity regulation. | For the second and third proposed mechanisms of action, Ectatomin has also been shown to inhibit kinases, specifically protein tyrosine kinase and protein kinase C, and Ca2+ channels. Kinase inhibition would potentially allow Ectatomin to interfere with various components of signal transduction. Calcium channel inhibition would potentially allow Ectatomin to affect physiological processes such as contraction, neurotransmitter release and neuronal activity regulation. | ||
[[Image:Possible_Ectatomin_Mechanism_3.png|300px|left|thumb| A proposed membrane insertion (above) and dimerization mechanism to form cation channel (below) of Ectatomin. Insertion occurs when the α and β subunits open at the hairpin hinge region, exposing internal hydrophobic residues which interact with hydrophobic lipid tails of the cell membrane. Pore formation occurs after dimerization, allowing ions to freely cross the membrane.]] | [[Image:Possible_Ectatomin_Mechanism_3.png|300px|left|thumb| A proposed membrane insertion (above) and dimerization mechanism to form cation channel (below) of Ectatomin. Insertion occurs when the α and β subunits open at the hairpin hinge region (shown in black with yellow disulfide bonds), exposing internal hydrophobic residues which interact with hydrophobic lipid tails of the cell membrane. Pore formation occurs after dimerization, allowing ions to freely cross the membrane.]] | ||
== Toxicology == | == Toxicology == | ||