Sandbox Reserved 970: Difference between revisions

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The <scene name='60/604489/Secondary_structure/1'>secondary structure</scene> of the protein is composed of helical regions (47%), beta sheet regions (16%) and loops. There are <scene name='60/604489/10_transmembrane_helices/1'>10 transmembrane alpha helices</scene>, and three of them line a channel that spans the lipid bilayer and that allows calcium to pass through membranes. It also contains too cytoplasmic loops between the transmembrane helices. When the protein is not phosphorylated, two of the transmembrane helices are disrupted and form a cavity that can bind two molecules of calcium.  
The <scene name='60/604489/Secondary_structure/1'>secondary structure</scene> of the protein is composed of helical regions (47%), beta sheet regions (16%) and loops. There are <scene name='60/604489/10_transmembrane_helices/1'>10 transmembrane alpha helices</scene>, and three of them line a channel that spans the lipid bilayer and that allows calcium to pass through membranes. It also contains too cytoplasmic loops between the transmembrane helices. When the protein is not phosphorylated, two of the transmembrane helices are disrupted and form a cavity that can bind two molecules of calcium.  


The protein is divided in <scene name='60/604489/The_4_domains_of_the_pump/1'>4 regions</scene>. The <scene name='60/604489/Transmembrane_domain/1'>transmembrane region</scene> of the protein contains the channel that span the lipid bilayer, and the calcium binding cavity.  
The protein is divided in <scene name='60/604489/The_4_domains_of_the_pump/1'>4 regions</scene>. The <scene name='60/604489/Transmembrane_domain/1'>transmembrane region</scene> of the protein contains the channel that spans the lipid bilayer, and the calcium binding cavity.  


The two cytoplasmic loops form three separate domains. The <scene name='60/604489/Nucleotide_binding_domain/1'>nucleotide binding domain (N)</scene> contains the site where ATP binds to the protein. The <scene name='60/604489/P_domain/1'>phosphorylation domain (P)</scene> contains an Aspartate residue (<scene name='60/604489/Asp_351/1'>Asp 351</scene>) that can be phosphorylated. Finally, the <scene name='60/604489/Actuator_domain/1'>actuator domain (A)</scene> is involved in the transmission of major conformational changes. The phosphorylation and the nucleotide binding domains form the <scene name='60/604489/Catalytic_site/1'>catalytic site</scene> of the protein<ref name="first">Benjamin Lewin, 2007 - Cells - Jones & Bartlett Learning</ref>.   
The two cytoplasmic loops form three separate domains. The <scene name='60/604489/Nucleotide_binding_domain/1'>nucleotide binding domain (N)</scene> contains the site where ATP binds to the protein. The <scene name='60/604489/P_domain/1'>phosphorylation domain (P)</scene> contains an Aspartate residue (<scene name='60/604489/Asp_351/1'>Asp 351</scene>) that can be phosphorylated. Finally, the <scene name='60/604489/Actuator_domain/1'>actuator domain (A)</scene> is involved in the transmission of major conformational changes. The phosphorylation and the nucleotide binding domains form the <scene name='60/604489/Catalytic_site/1'>catalytic site</scene> of the protein<ref name="first">Benjamin Lewin, 2007 - Cells - Jones & Bartlett Learning</ref>.