Sandbox GGC10
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=Sodium-Potassium Pump= | =Sodium-Potassium Pump= | ||
<StructureSection load='3B8E' size='340' side='right' caption='Na+/K+ Pump Protein' scene=''> | <StructureSection load='3B8E' size='340' side='right' caption='Na+/K+ Pump Protein' scene=''> | ||
+ | The Sodium Potassium Pump is important to the physiology of our bodies because it can be found in all human cells. This in turn helps maintain optimal ion balance. Hence, this is why our body uses one-fourth of its energy to power the pump and keep it regulating. | ||
== Function == | == Function == | ||
The primary function of this protein serves as the catalytic component of the active enzymes, which catalyzes the hydrolysis of the ATP coupled with the exchange of sodium and potassium across the plasma membrane. Additionally, this action potential assists in creating an electrochemical gradient of sodium and potassium ions by delivering the energy for the active transport of numerous nutrients.<ref>PMID:30725773</ref> Therefore, the NA+/K+ pump functions by having to transport sodium and potassium ions across the cell membrane in a 3 to 2 ratio (3 Na+ out and 2 K+ in). By doing this, the membrane potential increases its stability and therefore is essential in human cells as it constantly maintains an optimal ion balance.<ref>PMID:27490484</ref> In addition, the sodium-potassium pump functions in many systems. A high level of expression can be found in the kidneys as they are responsible for expressing 50 million pumps per cell to filter waste products in the blood, maintain optimal pH's, regulate electrolyte levels, and reabsorb glucose and amino acids. Another important place this ATPase activity can be seen is in the brain as the neurons need this pump to reverse postsynaptic sodium flux to activate action potentials.<ref>PMID:25566080</ref> | The primary function of this protein serves as the catalytic component of the active enzymes, which catalyzes the hydrolysis of the ATP coupled with the exchange of sodium and potassium across the plasma membrane. Additionally, this action potential assists in creating an electrochemical gradient of sodium and potassium ions by delivering the energy for the active transport of numerous nutrients.<ref>PMID:30725773</ref> Therefore, the NA+/K+ pump functions by having to transport sodium and potassium ions across the cell membrane in a 3 to 2 ratio (3 Na+ out and 2 K+ in). By doing this, the membrane potential increases its stability and therefore is essential in human cells as it constantly maintains an optimal ion balance.<ref>PMID:27490484</ref> In addition, the sodium-potassium pump functions in many systems. A high level of expression can be found in the kidneys as they are responsible for expressing 50 million pumps per cell to filter waste products in the blood, maintain optimal pH's, regulate electrolyte levels, and reabsorb glucose and amino acids. Another important place this ATPase activity can be seen is in the brain as the neurons need this pump to reverse postsynaptic sodium flux to activate action potentials.<ref>PMID:25566080</ref> | ||
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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: | + | 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> |
Current revision
Sodium-Potassium Pump
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References
- ↑ Pirahanchi Y, Jessu R, Aeddula NR. Physiology, Sodium Potassium Pump PMID:30725773
- ↑ Rui H, Artigas P, Roux B. The selectivity of the Na(+)/K(+)-pump is controlled by binding site protonation and self-correcting occlusion. Elife. 2016 Aug 4;5. doi: 10.7554/eLife.16616. PMID:27490484 doi:http://dx.doi.org/10.7554/eLife.16616
- ↑ Forrest MD. The sodium-potassium pump is an information processing element in brain computation. Front Physiol. 2014 Dec 23;5:472. doi: 10.3389/fphys.2014.00472. eCollection, 2014. PMID:25566080 doi:http://dx.doi.org/10.3389/fphys.2014.00472
- ↑ Funck VR, Ribeiro LR, Pereira LM, de Oliveira CV, Grigoletto J, Della-Pace ID, Fighera MR, Royes LF, Furian AF, Larrick JW, Oliveira MS. Contrasting effects of Na+, K+-ATPase activation on seizure activity in acute versus chronic models. Neuroscience. 2015 Jul 9;298:171-9. doi: 10.1016/j.neuroscience.2015.04.031. Epub, 2015 Apr 20. PMID:25907445 doi:http://dx.doi.org/10.1016/j.neuroscience.2015.04.031
- ↑ Lees GJ. Inhibition of sodium-potassium-ATPase: a potentially ubiquitous mechanism contributing to central nervous system neuropathology. Brain Res Brain Res Rev. 1991 Sep-Dec;16(3):283-300. doi:, 10.1016/0165-0173(91)90011-v. PMID:1665097 doi:http://dx.doi.org/10.1016/0165-0173(91)90011-v
- ↑ Clausen T. Clinical and therapeutic significance of the Na+,K+ pump*. Clin Sci (Lond). 1998 Jul;95(1):3-17. PMID:9662481
- ↑ Tack CJ, Lutterman JA, Vervoort G, Thien T, Smits P. Activation of the sodium-potassium pump contributes to insulin-induced vasodilation in humans. Hypertension. 1996 Sep;28(3):426-32. doi: 10.1161/01.hyp.28.3.426. PMID:8794828 doi:http://dx.doi.org/10.1161/01.hyp.28.3.426
- ↑ Shrimanker I, Bhattarai S. Electrolytes PMID:31082167
- ↑ Geering K. Functional roles of Na,K-ATPase subunits. Curr Opin Nephrol Hypertens. 2008 Sep;17(5):526-32. doi:, 10.1097/MNH.0b013e3283036cbf. PMID:18695395 doi:http://dx.doi.org/10.1097/MNH.0b013e3283036cbf
- ↑ Jorgensen PL, Andersen JP. Structural basis for E1-E2 conformational transitions in Na,K-pump and Ca-pump proteins. J Membr Biol. 1988 Jul;103(2):95-120. doi: 10.1007/BF01870942. PMID:3054114 doi:http://dx.doi.org/10.1007/BF01870942