Sandbox Reserved 1790: Difference between revisions

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OCA, Jaime Prilusky, Inaya Patel, Rushda Hussein, Madeline Gilbert

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 ==SHOC2 and PP1C==
-<scene name='95/952717/Shoc2_and_pp1c/1'>PP1C binds to SHOC2</scene> on its leucine rich region(LRR). Between LRR2 and LRR5 and between LRR7 and LRR11. Mutations between SHOC2 and PP1C to the LRR were shown to completely inhibit the binding of PP1C. Five main <scene name='95/952716/Shoc2_and_pp1c/3'>hydrogen bonds</scene> are made: E56-R182, E167-R203, E54-K180, R187-H178, R188-E155. The binding regions can also be shown as acidic and basic patches on <scene name='95/952718/Acid_base_pp1c/1'>PP1C</scene> and <scene name='95/952718/Acid_base_shoc2/2'>SHOC2</scene>. The corresponding patches interact to form a <scene name='95/952718/Acid_base_shoc2pp1c/1'>binary complex</scene>. These interactions do not result in significant conformational changes <ref name="Kwon">PMID:35831509</ref>.
+<scene name='95/952717/Shoc2_and_pp1c/1'>PP1C binds to SHOC2</scene> on its leucine rich region(LRR). Between LRR2 and LRR5 and between LRR7 and LRR11. Mutations between SHOC2 and PP1C to the LRR were shown to completely inhibit the binding of PP1C. Five main <scene name='95/952716/Shoc2_and_pp1c/3'>hydrogen and ionic bonds</scene> are made between PP1C and SHOC2 respectively: E56-R182, E167-R203, E54-K180, R187-H178, R188-E155 <ref name="Kwon">PMID:35831509</ref>. Reflecting this ionic character, the binding regions are contained within extensive acidic and basic patches on <scene name='95/952718/Acid_base_pp1c/1'>PP1C</scene> and <scene name='95/952718/Acid_base_shoc2/2'>SHOC2</scene>. The negative acidic patches of PP1C interact with the positive basic patches of SHOC2 and vice versa to form a <scene name='95/952718/Acid_base_shoc2pp1c/1'>binary complex</scene>. These interactions do not result in significant conformational changes to either protein <ref name="Kwon">PMID:35831509</ref>.
 ==SHOC2 and MRAS==
-MRAS is initially bound to GDP causing it to be in its inactive state. This form cannot bind to the SHOC2-PP1C complex due to steric clashing. Once GDP is exchanged for GTP to activate the protein, conformational changes occur within the switch I and switch II regions to allow <scene name='95/952716/Scho2-mras-interactions/2'>MRAS to interact with SHOC2</scene>. These <scene name='95/952716/Scho2-mras-interactions/1'>interactions</scene> include hydrogen bonds and pi stacking. The primary hydrogen bonds are R288-Q71 and R177-E47. Pi staking occurs at R104-R83 <ref name="Lavoie">Lavoie H, Therrien M. Structural keys unlock RAS-MAPK cellular signalling pathway. Nature. 2022 Sep;609(7926):248-249. [http://dx.doi.org/10.1038/d41586-022-02189-7 doi: 10.1038/d41586-022-02189-7. PMID: 35970881.]</ref>.
+MRAS is initially bound to GDP causing it to be in its inactive state. This form cannot bind to the SHOC2-PP1C complex due to steric clashing. Once GDP is exchanged for GTP to activate the protein, conformational changes occur within the switch I and switch II regions to allow <scene name='95/952716/Scho2-mras-interactions/2'>MRAS to interact with SHOC2</scene>. These <scene name='95/952716/Scho2-mras-interactions/1'>interactions</scene> include hydrogen bonds and pi stacking. The primary hydrogen bonds are R288-Q71 and R177-E47. Pi staking occurs at R104-R83 <ref name="Lavoie">Lavoie H, Therrien M. Structural keys unlock RAS-MAPK cellular signaling pathway. Nature. 2022 Sep;609(7926):248-249. [http://dx.doi.org/10.1038/d41586-022-02189-7 doi: 10.1038/d41586-022-02189-7. PMID: 35970881.]</ref>.
 ==PP1C and MRAS==