Sandbox Reserved 1336
From Proteopedia
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| - | + | =Lipid Scramblase nhTMEM16= | |
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==Structure== | ==Structure== | ||
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| - | + | <Structure load='4wis' size='350' frame='true' align='right' caption='Insert caption here' scene='' /> | |
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| + | <scene name='77/777656/Original_molecule/1'>Click here to see the original molecule.</scene> | ||
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| + | The lipid scramblase nhTMEM16 protein is a homo dimer, meaning its primary structure is composed of two identical chains. The defining feature of this protein is its calcium-activated chloride channels. The binding sites for these Ca2+ ions are located in the hydrophobic center of the molecule. These parts can be seen below, under the "structural highlights" section of this page. | ||
== Function == | == Function == | ||
| + | TMEM16 proteins are responsible for the eventual activation of platelets which is important for blood clotting. They are also responsible for the movement of phospholipids across the bilayer and even play an important role in apoptosis. | ||
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| + | Calcium-activated chloride channels are an important element in many mammalian excitable cells. They facilitate the passive diffusion of chlorine ions in and out of the cell, which helps regulate the membrane potential. | ||
== Disease == | == Disease == | ||
| + | Scott syndrome is a rare human disease caused by a mutation that affects TMEM16 proteins and results in the inability of platelets and other hematopoietic cells to bring phosphatidylserine to the surface for proper coagulation. | ||
== Relevance == | == Relevance == | ||
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| + | Though lipid scramblase nhTMEM16 is most significant for those with Scotts syndrome, it is highly important in all organisms due to its role in apoptosis. If it were not able to enable cell death, cancerous cell behavior would be highly prevalent and even more dangerous. | ||
== Structural highlights == | == Structural highlights == | ||
| + | This protein prefers to form homodimers, which means that the complex is made of two identical chains of itself. <scene name='77/777656/Singlechain/1'>Click here to see one chain.</scene> | ||
| - | + | There are multiple sites where calcium ions can bind. <scene name='77/777656/Ca_binding_sites/1'>Click here to see where these are.</scene> | |
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| + | Once Ca ions bind to these sites, the chloride channel can open. <scene name='77/777656/Ca-activated_chloride_channel/1'>Click here to see the Ca-activated chloride channel.</scene> | ||
| - | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
| + | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4737519/ | ||
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| + | https://www.rcsb.org/pdb/protein/C7Z7K1?addPDB=4WIS | ||
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| + | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3336373/ | ||
Current revision
Contents |
Lipid Scramblase nhTMEM16
Structure
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The lipid scramblase nhTMEM16 protein is a homo dimer, meaning its primary structure is composed of two identical chains. The defining feature of this protein is its calcium-activated chloride channels. The binding sites for these Ca2+ ions are located in the hydrophobic center of the molecule. These parts can be seen below, under the "structural highlights" section of this page.
Function
TMEM16 proteins are responsible for the eventual activation of platelets which is important for blood clotting. They are also responsible for the movement of phospholipids across the bilayer and even play an important role in apoptosis.
Calcium-activated chloride channels are an important element in many mammalian excitable cells. They facilitate the passive diffusion of chlorine ions in and out of the cell, which helps regulate the membrane potential.
Disease
Scott syndrome is a rare human disease caused by a mutation that affects TMEM16 proteins and results in the inability of platelets and other hematopoietic cells to bring phosphatidylserine to the surface for proper coagulation.
Relevance
Though lipid scramblase nhTMEM16 is most significant for those with Scotts syndrome, it is highly important in all organisms due to its role in apoptosis. If it were not able to enable cell death, cancerous cell behavior would be highly prevalent and even more dangerous.
Structural highlights
This protein prefers to form homodimers, which means that the complex is made of two identical chains of itself.
There are multiple sites where calcium ions can bind.
Once Ca ions bind to these sites, the chloride channel can open.
References
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4737519/
