Sandbox GGC10: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
The Sodium Potassium Pump is a transmembrane protein that consists of the alpha, beta, and FXYD Subunits. The alpha subunit consists of <scene name='User:Christopher_Koehn/sandbox_1/Monomer_with_labeled_domains/1'>three functional domains:</scene> The actuator domain (A), the nucleotide-binding domain (N), and the phosphorylation domain (P). These domains function in the rate of ion transports and signaling. The Beta subunit consists of a few gatherings of <scene name='User:Christopher_Koehn/sandbox_1/Beta_subunit_interactions/1'>aromatic residues</scene>. This is very crucial as this helps target the polypeptide to the membrane and overall improved stability.<ref>PMID:18695395</ref> Additionally, the Na+ K+ pump alternates between two conformations: E1 and E2. In the <scene name='User:Christopher_Koehn/sandbox_1/E2-p_structure/6'>E1 State</scene>, the ATP will be cleaved and the gamma phosphate will be moved to ASP376. The phosphate group is shown by an MgF4 Analog. In the <scene name='User:Christopher_Koehn/sandbox_1/E2-p_structure/2'>E2 state</scene>, the site of binding consists of THR779, SER782, ASN783, and ASP811. These function in creating a kink so that the K+ ion can bind to this site.<ref>PMID:3054114</ref>
The Sodium Potassium Pump is a transmembrane protein that consists of the alpha, beta, and FXYD Subunits. The alpha subunit consists of <scene name='User:Faizal/sandbox_10/Alpha_subunit/1'>three functional domains:</scene> The actuator domain (A), the nucleotide-binding domain (N), and the phosphorylation domain (P). These domains function in the rate of ion transports and signaling. The Beta subunit consists of a few gatherings of <scene name='User:Faizal/sandbox_10/Beta_subunit_interactions/1'>aromatic residues</scene>. This is very crucial as this helps target the polypeptide to the membrane and overall improved stability.<ref>PMID:18695395</ref> Additionally, the Na+ K+ pump alternates between two conformations: E1 and E2. In the <scene name='Faizal/sandbox_10/E1_structure/6'>E1 State</scene>, the ATP will be cleaved and the gamma phosphate will be moved to ASP376. The phosphate group is shown by an MgF4 Analog. In the <scene name='User:Faizal/sandbox_10/E2_structure/2'>E2 state</scene>, the site of binding consists of THR779, SER782, ASN783, and ASP811. These function in creating a kink so that the K+ ion can bind to this site.<ref>PMID:3054114</ref>




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