Sandbox WWC6: Difference between revisions
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<Structure load='7AHL' size='350' frame='true' align='right' caption='Stapholococcal alpha-hemolysin' scene='Insert optional scene name here' /> | <Structure load='7AHL' size='350' frame='true' align='right' caption='Stapholococcal alpha-hemolysin' scene='Insert optional scene name here' /> | ||
==Function== | ==Function== | ||
Hemolysins act through disruption of the cell membrane. Two main functions destroy phospholipid membranes: pore formation and phosphilipid hydrosysis. <ref>http://www.sciencedirect.com/science/article/pii/S0005273610002610</ref> Pore formation, the most common mechanism of hemolysin cell <ref name ="sod"/> This information was first discovered by Hodgkin and Huxley in 1952. <ref name ="physio">https://en.wikipedia.org/wiki/Hodgkin%E2%80%93Huxley_model</ref> For more information on the role of sodium channels in electrical signaling, click [https://en.wikipedia.org/wiki/Action_potential here]. | Hemolysins act through disruption of the cell membrane. Two main functions destroy phospholipid membranes: pore formation and phosphilipid hydrosysis. <ref>http://www.sciencedirect.com/science/article/pii/S0005273610002610</ref> Pore formation, the most common mechanism of hemolysin cell <ref name ="sod"/> This information was first discovered by Hodgkin and Huxley in 1952. <ref name ="physio">https://en.wikipedia.org/wiki/Hodgkin%E2%80%93Huxley_model</ref> For more information on the role of sodium channels in electrical signaling, click [https://en.wikipedia.org/wiki/Action_potential here]. | ||
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==Structure== | ==Structure== | ||
Hemolysins have three structural variations: alpha, beta, and gamma. These hemolysin types are comprised of hepta or octomeric subunits.<ref name = "sod"/> The alpha subunit, depicted right, consists of four repeating structures, named I through IV and shown in different colors <scene name='69/696300/Right_one/1'>here</scene>. <ref name ="struct"> DOI: 10.1111/j.1469-7793.1998.647bp.x </ref> These structures consist of six transmembrane alpha helices named S1 through S6. <ref name = "struct"/> Interestingly, each repeating subunit resembles a bacterial K<sup>+</sup> channel. <ref name = "struct"/> These subunits fold together to form a central pore, and this complete structure resembles a bacterial Ca2<sup>+</sup> channel. <ref name = "struct"/> | Hemolysins have three structural variations: alpha, beta, and gamma. These hemolysin types are comprised of hepta or octomeric subunits.<ref name = "sod"/> The alpha subunit, depicted right, consists of four repeating structures, named I through IV and shown in different colors <scene name='69/696300/Right_one/1'>here</scene>. <ref name ="struct"> DOI: 10.1111/j.1469-7793.1998.647bp.x </ref> These structures consist of six transmembrane alpha helices named S1 through S6. <ref name = "struct"/> Interestingly, each repeating subunit resembles a bacterial K<sup>+</sup> channel. <ref name = "struct"/> These subunits fold together to form a central pore, and this complete structure resembles a bacterial Ca2<sup>+</sup> channel. <ref name = "struct"/> | ||
<scene name='69/696302/Beta-hemolysin/1'> | |||
<scene name='69/696302/Alpha-hemolysin/1'>Alpha-hemolysin</scene> | |||
<scene name='69/696302/Beta-hemolysin/1'>Gamma-hemolysin</scene> | |||
[[Image:640px-Sodium-channel.png]] | [[Image:640px-Sodium-channel.png]] | ||