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<scene name='95/952717/Shoc2/1'>SHOC2</scene> is a scaffold protein that is composed of 20 leucine-rich repeat domains that form a solenoid structure. The leucine rich region forms a concave hydrophobic core which is necessary for binding with PP1C and MRAS. | <scene name='95/952717/Shoc2/1'>SHOC2</scene> is a scaffold protein that is composed of 20 leucine-rich repeat domains that form a solenoid structure. The leucine rich region forms a concave hydrophobic core which is necessary for binding with PP1C and MRAS. | ||
=== PP1C === | === PP1C === | ||
| - | <scene name='95/952717/Pp1c/1'>PP1C</scene> is a catalytic protein. After forming a ternary complex, the | + | <scene name='95/952717/Pp1c/1'>PP1C</scene> is a catalytic protein. After forming a ternary complex, the <scene name='95/952717/Pp1c_hydrophobic_patch/1'>hydrophobic active site</scene> on the protein interacts with Raf to act as a phosphatase and dephosphorylate Ser 259. |
=== MRAS === | === MRAS === | ||
<scene name='95/952717/Mras/2'>MRAS</scene> is a membrane bound structure that aids the complex in localizing near other structures such as the RAS-RAF-MAPK complex in order to initiate downstream signaling. In its inactive state, MRAS is bound to GDP. When signaled by growth factors, the GDP is exchanged for GTP. The now <scene name='95/952718/Zoom_in_gtp/1'>GTP bound MRAS</scene> undergoes a conformational change of the switch I and switch II regions. This conformational change activates the protein allowing it to bind more easily with the SHOC2-PP1C complex. In comparison to other RAS proteins, MRAS has a greater affinity for the SHOC2-PP1C complex. | <scene name='95/952717/Mras/2'>MRAS</scene> is a membrane bound structure that aids the complex in localizing near other structures such as the RAS-RAF-MAPK complex in order to initiate downstream signaling. In its inactive state, MRAS is bound to GDP. When signaled by growth factors, the GDP is exchanged for GTP. The now <scene name='95/952718/Zoom_in_gtp/1'>GTP bound MRAS</scene> undergoes a conformational change of the switch I and switch II regions. This conformational change activates the protein allowing it to bind more easily with the SHOC2-PP1C complex. In comparison to other RAS proteins, MRAS has a greater affinity for the SHOC2-PP1C complex. | ||
Revision as of 00:11, 7 April 2023
This page, as it appeared on March 17, 2023, was featured in this article in the journal Biochemistry and Molecular Biology Education.
SHOC2-PP1C-MRAS
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