Sandbox Reserved 1776

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blue link LRR [https://en.wikipedia.org/wiki/Leucine-rich_repeat LRR]
blue link LRR [https://en.wikipedia.org/wiki/Leucine-rich_repeat LRR]
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Arkun (for ERK signaling) <Ref name= 'Arkun'> Arkun, Y., & Yasemi, M. Dynamics and control of the ERK signaling pathway: Sensitivity, bistability, and oscillations. PloS one, 13(4), e0195513. doi: 10.1371/journal.pone.0195513 [https://doi.org/10.1371/journal.pone.0195513. DOI: 10.1371/journal.pone.0195513]. </Ref>
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For last sentence in implications van der Burgt <Ref name= 'van der Burgt'> van der Burgt, I. Noonan syndrome. Orphanet J Rare Dis 2, 4 (2007). doi: 10.1186/1750-1172-2-4 [https://doi.org/10.1186/1750-1172-2-4. DOI: 10.1186/1750-1172-2-4]. </Ref>
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PP1C REF: <Ref name= 'Aggen'> Aggen, J., Nairn, A., Chamberlin, R. Regulation of protein phosphatase-1. Chemistry & Biology 2000, 7:R13–R23. [https://www.cell.com/cell-chemical-biology/pdf/S1074-5521(00)00069-7.pdf]. </Ref>.
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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.
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.
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Current revision

This Sandbox is Reserved from February 27 through August 31, 2023 for use in the course CH462 Biochemistry II taught by R. Jeremy Johnson at the Butler University, Indianapolis, USA. This reservation includes Sandbox Reserved 1765 through Sandbox Reserved 1795.
To get started:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing

Your Heading Here (maybe something like 'Structure')

SHOC2-PP1C-MRAS holoenzyme complex

Drag the structure with the mouse to rotate

References

  1. ↑ 1.0 1.1 Bernal Astrain G, Nikolova M, Smith MJ. Functional diversity in the RAS subfamily of small GTPases. Biochem Soc Trans. 2022 Apr 29;50(2):921-933. doi: 10.1042/BST20211166. DOI:10.1042/BST20211166.
  2. ↑ Molina JR, Adjei AA. The Ras/Raf/MAPK pathway. J Thorac Oncol. 2006 Jan;1(1):7-9. DOI:10.1016/S1556-0864(15)31506-9.
  3. ↑ 3.0 3.1 3.2 Hauseman, Z.J., Fodor, M., Dhembi, A. et al. Structure of the MRAS–SHOC2–PP1C phosphatase complex. Nature 609, 416–423 (2022). doi: 10.1038/s41586-022-05086-1. DOI:10.1038/s41586-022-05086-1.
  4. ↑ Liau, N.P.D., Johnson, M.C., Izadi, S. et al. Structural basis for SHOC2 modulation of RAS signalling. Nature 609, 400–407 (2022).doi: 10.1038/s41586-022-04838-3. DOI:10.1038/s41586-022-04838-3.
  5. ↑ Kwon, J.J., Hajian, B., Bian, Y. et al. Structure–function analysis of the SHOC2–MRAS–PP1C holophosphatase complex. Nature 609, 408–415 (2022).doi: 10.1038/s41586-022-04928-2. DOI:10.1038/s41586-022-04928-2.
  6. ↑ Lavoie, H., Therrien, M. Structural keys unlock RAS–MAPK cellular signalling pathway. Nature 609, 248-249 (2022). doi: 10.1038/d41586-022-02189-7. DOI:10.1038/d41586-022-02189-7.
  7. ↑ Kwon, J., Jajian, B., Bian, Y. et al. Comprehensive structure-function evaluation of the SHOC2 holophosphatase reveals disease mechanisms and therapeutic opportunities. In: Proceedings of the American Association for Cancer Research Annual Meeting 2022. DOI: 10.1158/1538-7445.AM2022-LB029.
  8. ↑ Bonsor, D., Alexander, P., Snead, K. et al. Structure of the SHOC2–MRAS–PP1C complex provides insights into RAF activation and Noonan syndrome. Nat Struct Mol Biol 29, 966–977 (2022). doi:10.1038/s41594-022-00841-4. DOI: 10.1038/s41594-022-00841-4.
  9. ↑ Young, L., Rodriguez-Viciana, P. MRAS: A Close but Understudied Member of the RAS Family. Cold Spring Harbor Perspectives in Medicine (2018). doi: 10.1101/cshperspect.a033621. DOI: 0.1101/cshperspect.a033621.
  10. ↑ Kwon, J. J., & Hahn, W. C. A Leucine-Rich Repeat Protein Provides a SHOC2 the RAS Circuit: a Structure-Function Perspective. Molecular and cellular biology, 41(4), e00627-20 (2021). doi:10.1128/MCB.00627-20. DOI: 10.1128/MCB.00627-20.
  11. ↑ Arkun, Y., & Yasemi, M. Dynamics and control of the ERK signaling pathway: Sensitivity, bistability, and oscillations. PloS one, 13(4), e0195513. doi: 10.1371/journal.pone.0195513 DOI: 10.1371/journal.pone.0195513.
  12. ↑ van der Burgt, I. Noonan syndrome. Orphanet J Rare Dis 2, 4 (2007). doi: 10.1186/1750-1172-2-4 DOI: 10.1186/1750-1172-2-4.
  13. ↑ Aggen, J., Nairn, A., Chamberlin, R. Regulation of protein phosphatase-1. Chemistry & Biology 2000, 7:R13–R23. [1].
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