Sandbox Reserved 1777: Difference between revisions

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==Overview==

The complex combines three separate proteins, SHOC2, PP1C, and MRAS, to form the active protein (SMP complex), as seen in Figure 2<Ref name='Hauseman'>Hauseman, Z.J., Fodor, M., Dhembi, A. et al. Structure of the MRAS–SHOC2–PP1C phosphatase complex. Nature 609, 416–423 (2022). doi: 10.1038/s41586-022-05086-1. [https://doi.org/10.1038/s41586-022-05086-1. DOI:10.1038/s41586-022-05086-1]. </Ref>. In complex, each of these proteins are responsible for a different role. MRAS is the "on and off" switch; when MRAS is activated from binding GTP, ~~'''fill in here'''.~~ PP1C ~~by itself is a catalytic enzyme that ''' fill in here'''~~. In complex, PP1C is tasked with being the catalytic domain and removing a phosphate from RAF. The last piece of the complex is SHOC2, which is responsible for holding and stabilizing MRAS and PP1C <Ref name= 'Hahn'> Kwon, J. J., & Hahn, W. C. A Leucine-Rich Repeat Protein Provides a SHOC2 the RAS Circuit: a Structure-Function Perspective. Molecular and cellular biology, 41(4), e00627-20 (2021). doi:10.1128/MCB.00627-20. [http://doi.org/10.1128/MCB.00627-20. DOI: 10.1128/MCB.00627-20]. </Ref>. The SMP complex was determined via cryo-electron microscopy as well as x-ray diffraction. The overall architecture has PP1C and MRAS bound within the concave surface of SHOC2, leaving the catalytic site of PP1C and the GTP binding cleft in MRAS exposed.

The complex combines three separate proteins, SHOC2, PP1C, and MRAS, to form the active protein (SMP complex), as seen in Figure 2<Ref name='Hauseman'>Hauseman, Z.J., Fodor, M., Dhembi, A. et al. Structure of the MRAS–SHOC2–PP1C phosphatase complex. Nature 609, 416–423 (2022). doi: 10.1038/s41586-022-05086-1. [https://doi.org/10.1038/s41586-022-05086-1. DOI:10.1038/s41586-022-05086-1]. </Ref>. In complex, each of these proteins are responsible for a different role. MRAS is the "on and off" switch; when MRAS is activated from binding GTP, it recruits SHOC2 and PP1C for complex formation. In complex, PP1C is tasked with being the catalytic domain and removing a phosphate from RAF. The last piece of the complex is SHOC2, which is responsible for holding and stabilizing MRAS and PP1C <Ref name= 'Hahn'> Kwon, J. J., & Hahn, W. C. A Leucine-Rich Repeat Protein Provides a SHOC2 the RAS Circuit: a Structure-Function Perspective. Molecular and cellular biology, 41(4), e00627-20 (2021). doi:10.1128/MCB.00627-20. [http://doi.org/10.1128/MCB.00627-20. DOI: 10.1128/MCB.00627-20]. </Ref>. The SMP complex was determined via cryo-electron microscopy as well as x-ray diffraction. The overall architecture has PP1C and MRAS bound within the concave surface of SHOC2, leaving the catalytic site of PP1C and the GTP binding cleft in MRAS exposed.

==SHOC2==

Sandbox Reserved 1777: Difference between revisions

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 ==Overview==
-The complex combines three separate proteins, SHOC2, PP1C, and MRAS, to form the active protein (SMP complex), as seen in Figure 2<Ref name='Hauseman'>Hauseman, Z.J., Fodor, M., Dhembi, A. et al. Structure of the MRAS–SHOC2–PP1C phosphatase complex. Nature 609, 416–423 (2022). doi: 10.1038/s41586-022-05086-1. [https://doi.org/10.1038/s41586-022-05086-1. DOI:10.1038/s41586-022-05086-1]. </Ref>. In complex, each of these proteins are responsible for a different role. MRAS is the "on and off" switch; when MRAS is activated from binding GTP, '''fill in here'''. PP1C by itself is a catalytic enzyme that ''' fill in here'''. In complex, PP1C is tasked with being the catalytic domain and removing a phosphate from RAF. The last piece of the complex is SHOC2, which is responsible for holding and stabilizing MRAS and PP1C <Ref name= 'Hahn'> Kwon, J. J., & Hahn, W. C. A Leucine-Rich Repeat Protein Provides a SHOC2 the RAS Circuit: a Structure-Function Perspective. Molecular and cellular biology, 41(4), e00627-20 (2021). doi:10.1128/MCB.00627-20. [http://doi.org/10.1128/MCB.00627-20. DOI: 10.1128/MCB.00627-20]. </Ref>. The SMP complex was determined via cryo-electron microscopy as well as x-ray diffraction. The overall architecture has PP1C and MRAS bound within the concave surface of SHOC2, leaving the catalytic site of PP1C and the GTP binding cleft in MRAS exposed.
+The complex combines three separate proteins, SHOC2, PP1C, and MRAS, to form the active protein (SMP complex), as seen in Figure 2<Ref name='Hauseman'>Hauseman, Z.J., Fodor, M., Dhembi, A. et al. Structure of the MRAS–SHOC2–PP1C phosphatase complex. Nature 609, 416–423 (2022). doi: 10.1038/s41586-022-05086-1. [https://doi.org/10.1038/s41586-022-05086-1. DOI:10.1038/s41586-022-05086-1]. </Ref>. In complex, each of these proteins are responsible for a different role. MRAS is the "on and off" switch; when MRAS is activated from binding GTP, it recruits SHOC2 and PP1C for complex formation. In complex, PP1C is tasked with being the catalytic domain and removing a phosphate from RAF. The last piece of the complex is SHOC2, which is responsible for holding and stabilizing MRAS and PP1C <Ref name= 'Hahn'> Kwon, J. J., & Hahn, W. C. A Leucine-Rich Repeat Protein Provides a SHOC2 the RAS Circuit: a Structure-Function Perspective. Molecular and cellular biology, 41(4), e00627-20 (2021). doi:10.1128/MCB.00627-20. [http://doi.org/10.1128/MCB.00627-20. DOI: 10.1128/MCB.00627-20]. </Ref>. The SMP complex was determined via cryo-electron microscopy as well as x-ray diffraction. The overall architecture has PP1C and MRAS bound within the concave surface of SHOC2, leaving the catalytic site of PP1C and the GTP binding cleft in MRAS exposed.
 ==SHOC2==