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{{Ectatomin 1eci}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | {{Ectatomin 1eci}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
==Ectatomin (1eci)== | ==Ectatomin (1eci)== | ||
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<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]. 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]. | Ectatomin (1eci) is the main component of venom of the ant [https://en.wikipedia.org/wiki/Ectatomma_tuberculatum Ectatomma tuberculatum]. 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]. | ||
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Biologically, Ectatomin exists as a heterodimer stabilized by <scene name='69/691538/Cysteine_disulfide/1'>disulfide</scene> linkages. The α subunit has 37 amino acid residues, while the β subunit has 34 amino acid residues. The structure of Ectatomin was solved using 2D NMR and CHARMm computational optimization, though there are 20 similar proposed conformations. | Biologically, Ectatomin exists as a heterodimer stabilized by <scene name='69/691538/Cysteine_disulfide/1'>disulfide</scene> linkages. The α subunit has 37 amino acid residues, while the β subunit has 34 amino acid residues. The structure of Ectatomin was solved using 2D NMR and CHARMm computational optimization, though there are 20 similar proposed conformations. | ||
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Generally, each subunit is composed of two α-helices, linked by disulfide bonds, with a connecting hairpin hinge region. The two subunits are linked by a disfulide bond between their hairpin hinge regions. One α-helix from each subunit is kinked, due to the presence of proline residues. The kinked α-helix of the α subunit is more kinked, containing three proline residues, while the kinked α-helix of the β subunit only contains one proline residue. | Generally, each subunit is composed of two α-helices, linked by disulfide bonds, with a connecting hairpin hinge region. The two subunits are linked by a disfulide bond between their hairpin hinge regions. One α-helix from each subunit is kinked, due to the presence of proline residues. The kinked α-helix of the α subunit is more kinked, containing three proline residues, while the kinked α-helix of the β subunit only contains one proline residue. | ||
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The internal region between the two subunits is primarily composed of hydrophobic residues. | The internal region between the two subunits is primarily composed of hydrophobic residues. | ||
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Sequence - α subunit | Sequence - α subunit | ||
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Sequence - β subunit | Sequence - β subunit | ||
WSTIVKLTICPTLKSMAKKCEGSIATMIKKKCDK | WSTIVKLTICPTLKSMAKKCEGSIATMIKKKCDK | ||
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== Mechanism == | == Mechanism == | ||
| - | Ectatomin has several proposed mechanisms of action. The primary proposed mechanism involves the formation of a nonselective cation channel. In this mechanism, the α and β subunits open up, exposing the internal hydrophobic residues. The protein flattens while remaining attached at the hairpin hinge region. The now exposed hydrophobic residues nonselectively insert into plasma membranes. The inserted protein dimerizes, eventually | + | Ectatomin has several proposed mechanisms of action. The primary proposed mechanism involves the formation of a nonselective cation channel. In this mechanism, the α and β subunits open up, exposing the internal hydrophobic residues. The protein flattens while remaining attached at the hairpin hinge region. The now exposed hydrophobic residues nonselectively insert into plasma membranes. The inserted protein dimerizes, eventually forming a nonselective cation channel. |
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. | ||
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== Toxicology == | == Toxicology == | ||
Revision as of 23:12, 25 February 2015
Ectatomin (1eci)
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