Sandbox Reserved 1767: Difference between revisions
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== Structure of Subunits == | == Structure of Subunits == | ||
=== SHOC2 === | === SHOC2 === | ||
<scene name='95/952695/Shoc2intro/1'>SHOC2</scene> is essential for complex formation. It is a crescent shaped complex that serves as a bridge for PP1C and MRAS, maximizing interaction between the three subunits of the SMP complex <ref name="Hauseman">PMID:35830882</ref>. SHOC2 contains a large leucine rich region (LRR) that provides stability and localizes subunit PP1C to the membrane<ref name="Liau">PMID: 35768504</ref>. SHOC2 only undergoes a <scene name='95/952693/Shoc2_gtp_bound_vs_gdp_bound/7'>6° conformational change</scene> when PP1C and MRAS bind showing it is a scaffolding protein that provides a favorable interface for complex formation<ref name="Liau">PMID: 35768504</ref>. SHOC2 depletion is being studied as a therapeutic approach for RAS-driven cancers due to large scale interactions of the subunits being made possible by SHOC2 <ref name="Kwon">PMID: 35831509</ref>. As shown in '''Figure 1 '''SHOC2 and PP1C first engage in binding with each other via an N-terminal <scene name='95/952695/Rvxf_motif/2'>RVXF Motif</scene> on SHOC2 that is complimentary to a binding sequence on PP1C. SHOC2 residues <scene name='95/952695/Shoc2_highlighted_residues/1'>V64 and F66</scene> embed in the complimentary region of PP1C, enhancing SHOC2 affinity for PP1C. SHOC2 binds MRAS-GTP through β strands of a LRR that interacts with a [https:// | <scene name='95/952695/Shoc2intro/1'>SHOC2</scene> is essential for complex formation. It is a crescent shaped complex that serves as a bridge for PP1C and MRAS, maximizing interaction between the three subunits of the SMP complex <ref name="Hauseman">PMID:35830882</ref>. SHOC2 contains a large leucine rich region (LRR) that provides stability and localizes subunit PP1C to the membrane<ref name="Liau">PMID: 35768504</ref>. SHOC2 only undergoes a <scene name='95/952693/Shoc2_gtp_bound_vs_gdp_bound/7'>6° conformational change</scene> when PP1C and MRAS bind showing it is a scaffolding protein that provides a favorable interface for complex formation<ref name="Liau">PMID: 35768504</ref>. SHOC2 depletion is being studied as a therapeutic approach for RAS-driven cancers due to large scale interactions of the subunits being made possible by SHOC2 <ref name="Kwon">PMID: 35831509</ref>. As shown in '''Figure 1 '''SHOC2 and PP1C first engage in binding with each other via an N-terminal <scene name='95/952695/Rvxf_motif/2'>RVXF Motif</scene> on SHOC2 that is complimentary to a binding sequence on PP1C. SHOC2 residues <scene name='95/952695/Shoc2_highlighted_residues/1'>V64 and F66</scene> embed in the complimentary region of PP1C, enhancing SHOC2 affinity for PP1C. SHOC2 binds MRAS-GTP through β strands of a LRR that interacts with a [https://pubmed.ncbi.nlm.nih.gov/21954777/. hydrophobic] region of MRAS-GTP further stabilizing the complex<ref name="Kwon">PMID: 35831509</ref>. | ||
=== PP1C === | === PP1C === | ||
[[Image:CS.png|300 px|right|thumb|'''Figure 2:''' Catalytic Site of PP1C (PDB 7DSO) <ref name="Liau">PMID: 35768504</ref>.]] | [[Image:CS.png|300 px|right|thumb|'''Figure 2:''' Catalytic Site of PP1C (PDB 7DSO) <ref name="Liau">PMID: 35768504</ref>.]] | ||