Sandbox GGC10

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== Structural highlights ==
== Structural highlights ==
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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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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>

Revision as of 19:41, 28 April 2021

Sodium-Potassium Pump

Na+/K+ Pump Protein

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References

  1. Pirahanchi Y, Jessu R, Aeddula NR. Physiology, Sodium Potassium Pump PMID:30725773
  2. 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
  3. 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
  4. 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
  5. 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
  6. Clausen T. Clinical and therapeutic significance of the Na+,K+ pump*. Clin Sci (Lond). 1998 Jul;95(1):3-17. PMID:9662481
  7. 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
  8. Shrimanker I, Bhattarai S. Electrolytes PMID:31082167
  9. 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
  10. 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
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