Sandbox Reserved 1777: Difference between revisions

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==PP1C==

<scene name='95/952705/Pp1c_structure/1'>PP1C</scene> is the catalytic domain of the phosphatase enzyme [https://www.ncbi.nlm.nih.gov/gene/5499 PP1], which removes reversible phosphorylations from signaling proteins. PP1C is a serine/threonine phosphatase involved in signaling pathways that control cell growth, division, and metabolism<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>. The '''[[ACTIVE SITE]]''' of PP1C is adjacent to a hydrophobic patch where it binds to the N-terminal phosphoserine of RAF, its target for dephosphorylation. PP1C has phosphatase activity in the absence of the ternary complex, but it lacks ~~the~~ intrinsic substrate selectivity<ref name="Hauseman" />. This indicates that the ~~whole~~ complex formation is necessary for PP1C's specificity for RAF.

<scene name='95/952705/Pp1c_structure/1'>PP1C</scene> is the catalytic domain of the phosphatase enzyme [https://www.ncbi.nlm.nih.gov/gene/5499 PP1], which removes reversible phosphorylations from signaling proteins. PP1C is a serine/threonine phosphatase involved in signaling pathways that control cell growth, division, and metabolism<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>. The '''[[ACTIVE SITE]]''' of PP1C is adjacent to a hydrophobic patch, where it binds to the N-terminal phosphoserine of RAF, its target for dephosphorylation. PP1C has phosphatase activity in the absence of the ternary complex, but it lacks intrinsic substrate selectivity<ref name="Hauseman" />. This indicates that the complex formation is necessary for PP1C's specificity for RAF.

==MRAS==

Sandbox Reserved 1777: Difference between revisions

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 ==PP1C==
-<scene name='95/952705/Pp1c_structure/1'>PP1C</scene> is the catalytic domain of the phosphatase enzyme [https://www.ncbi.nlm.nih.gov/gene/5499 PP1], which removes reversible phosphorylations from signaling proteins. PP1C is a serine/threonine phosphatase involved in signaling pathways that control cell growth, division, and metabolism<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>. The '''[[ACTIVE SITE]]''' of PP1C is adjacent to a hydrophobic patch where it binds to the N-terminal phosphoserine of RAF, its target for dephosphorylation. PP1C has phosphatase activity in the absence of the ternary complex, but it lacks the intrinsic substrate selectivity<ref name="Hauseman" />. This indicates that the whole complex formation is necessary for PP1C's specificity for RAF.
+<scene name='95/952705/Pp1c_structure/1'>PP1C</scene> is the catalytic domain of the phosphatase enzyme [https://www.ncbi.nlm.nih.gov/gene/5499 PP1], which removes reversible phosphorylations from signaling proteins. PP1C is a serine/threonine phosphatase involved in signaling pathways that control cell growth, division, and metabolism<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>. The '''[[ACTIVE SITE]]''' of PP1C is adjacent to a hydrophobic patch, where it binds to the N-terminal phosphoserine of RAF, its target for dephosphorylation. PP1C has phosphatase activity in the absence of the ternary complex, but it lacks intrinsic substrate selectivity<ref name="Hauseman" />. This indicates that the complex formation is necessary for PP1C's specificity for RAF.
 ==MRAS==