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From Proteopedia

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Contents 1 Structure 2 Function 3 Disease 4 Relevance 5 Structural highlights 6 References

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

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/

https://www.rcsb.org/pdb/protein/C7Z7K1?addPDB=4WIS