Sandbox GGC10: Difference between revisions

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== 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 clusters 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. 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. 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.

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 clusters 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. 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.

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>

== References ==

Sandbox GGC10: Difference between revisions

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@@ Line 11: / Line 11: @@
 == 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 clusters 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. 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. 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.
+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 clusters 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. 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.
-This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
 </StructureSection>
 == References ==
 <references/>