Sandbox Reserved 1336
From Proteopedia
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== 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 == | ||
Revision as of 21:31, 20 February 2018
Contents |
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
Platlet formation/clotting
Phospholipid movement
Apoptosis
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.
