Sandbox Reserved 1788: Difference between revisions
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<scene name='95/952717/Shoc2/1'>SHOC2</scene> is a crescent-shaped 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. SHOC2 is the crucial mediator for SHOC2-PP1C-MRAS complex formation. | <scene name='95/952717/Shoc2/1'>SHOC2</scene> is a crescent-shaped 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. SHOC2 is the crucial mediator for SHOC2-PP1C-MRAS complex formation. | ||
==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_hydrophobic_patch/1'>hydrophobic active site</scene> on the protein interacts with Raf to act as a phosphatase and dephosphorylate Ser 259. PP1C's active site is adjacent to a hydrophobic patch. It's theorized that the hydrophobic patch binds to the C-terminal of | <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. PP1C's active site is adjacent to a hydrophobic patch. It's theorized that the hydrophobic patch binds to the C-terminal of NTpS on RAF, the target for dephosphorylation. PP1C can act as a phosphatase in the absence of SHOC2 but PP1C lasks intrinsic substrate selectively. So SMP complex formation is necessary for PP1C specificity to RAF. | ||
[[Image:ActiveSiteProto.png|500 px|]] | [[Image:ActiveSiteProto.png|500 px|]] | ||
== MRAS == | == MRAS == | ||