Sandbox Reserved 1778

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=== SHOC2 ===
=== SHOC2 ===
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leucine rich repeat domain
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SHOC2 is a domain which acts as a cradle to bind PP1C and MRAS. The
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<scene name='95/952706/Shoc2_structure/1'>SHOC2 Structure</scene>
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<scene name='95/952706/Shoc2_structure/1'>Structure of SHOC2</scene>
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is a leucine rich repeat (LRR) protein that consists of 20 consecutive LRR domains. It is stabilized by an asparagine ladder and this motif results in an extended beta sheet on the inner concavity of the protein surface with alpha helices facing outward. This results in a largely hydrophobic core.
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=== MRAS ===
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<scene name='95/952706/Mras_structure/1'>MRAS</scene>
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binds to SHOC2 primarily by the descending loop and strands of each LRR domains 2-10. Once associated with SHOC2, it binds to PP1C and guides the holoenzyme complex to the cell membrane to begin signaling.
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=== MRAS ===
 
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does not bind PP1C in absence of SHOC2
 
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<scene name='95/952706/Mras_structure/1'>MRAS Structure</scene>
 
=== PP1C ===
=== PP1C ===
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protein phosphatase 1 catalytic subunit
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protein phosphatase 1 catalytic subunit (PP1C) is highly characterized of serine/ threonine phosphatase.
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<scene name='95/952706/Pp1c_structure/1'>PP1C Structure</scene>
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<scene name='95/952706/Pp1c_structure/1'>PP1C</scene>
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associates with the ascending loops of the SHOC2 LRR regions.
= Interactions =
= Interactions =

Revision as of 19:56, 27 March 2023

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.
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References

  1. ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
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