Sandbox Reserved 1653: Difference between revisions
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<StructureSection load='5z10' size='350' side='right' caption='Piezo 1' scene=''> | <scene name='86/868186/K2479_f2480/1'>Text To Be Displayed</scene><StructureSection load='5z10' size='350' side='right' caption='Piezo 1' scene=''> | ||
Piezo proteins constitute a family of excitatory [[ion channels]] directly gated by mechanical forces. Piezo is functionally conserved and very important | Piezo proteins constitute a family of excitatory [[ion channels]] directly gated by mechanical forces. Piezo is functionally conserved and very important | ||
because all living organisms are subjected to mechanical forces from their environment for instance [https://en.wikipedia.org/wiki/Proprioception proprioception], [https://en.wikipedia.org/wiki/Osmoregulation osmoregulation], vascular tone, | because all living organisms are subjected to mechanical forces from their environment for instance [https://en.wikipedia.org/wiki/Proprioception proprioception], [https://en.wikipedia.org/wiki/Osmoregulation osmoregulation], vascular tone, | ||
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==='''Ion conducting pore'''=== | ==='''Ion conducting pore'''=== | ||
The <scene name='86/868186/Ion_conducting_pore/1'>central pore axis</scene> of piezo1 is lined with the <scene name='86/868186/Ced/1'>extracellular cap domain</scene>, inner helix and cytosolic <scene name='86/868186/Ctd/1'>CTD</scene>. The extracellular cations can approach the pore entry “vertically through the internal cavity along the threefold axis of the cap domain”, they can also approach laterally through spaces (gaps) between the flexible linkers which connect the cap with inner and outer helices.<ref name= "ion channel"> DOI 10.1038/nature25453</ref> The <scene name='86/868186/Ion_conducting_pore/1'>ion conduction pathway</scene> is situated below the <scene name='86/868186/Ced/1'>cap</scene>, and is | The <scene name='86/868186/Ion_conducting_pore/1'>central pore axis</scene> of piezo1 is lined with the <scene name='86/868186/Ced/1'>extracellular cap domain</scene>, inner helix and cytosolic <scene name='86/868186/Ctd/1'>CTD</scene>. The extracellular cations can approach the pore entry “vertically through the internal cavity along the threefold axis of the cap domain”, they can also approach laterally through spaces (gaps) between the flexible linkers which connect the cap with inner and outer helices.<ref name= "ion channel"> DOI 10.1038/nature25453</ref> The <scene name='86/868186/Ion_conducting_pore/1'>ion conduction pathway</scene> is situated below the <scene name='86/868186/Ced/1'>cap</scene>, and is | ||
lined by the three inner transmembrane helices. The possible access for lipids or other hydrophobic molecules through the pore could be “two lateral openings between the inner helices separated by a ‘seal’ formed by K2479 and | lined by the three inner transmembrane helices. The possible access for lipids or other hydrophobic molecules through the pore could be “two lateral openings between the inner helices separated by a ‘seal’ formed by <scene name='86/868186/K2479_f2480/1'>K2479 and F2480</scene>”. These openings are approximately 11 Å wide and 16 Å tall. <ref name= "ion channel"> | ||
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<scene name='86/868186/E_dans_ctd/1'>E CTD</scene> | <scene name='86/868186/E_dans_ctd/1'>E CTD</scene> | ||
<scene name='86/868186/Ctd/1'>CTD</scene> | <scene name='86/868186/Ctd/1'>CTD</scene> | ||
<scene name='86/868186/K2479_f2480/1'>K et F</scene> | |||
</StructureSection> | </StructureSection> | ||
