Sandbox Reserved 1766: Difference between revisions

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There is a direct interaction between the RVXF motif of SHOC2 and the RVXF-binding pocket of PP1C.<ref name="Hauseman">PMID:35830882</ref>

SHOC2 has a RVxF binding motif that interacts with the PP1C RVxF binding site. The N-terminal loop of SHOC2 interacts with the RVxF binding site of PP1C, highlighting the structure and function connection of the complex. RVxF allows PP1C substrates to bind, whereas RAF has the RVxF motif, so it can bind to the hydrophobic region of SHOC2, allowing for greater specificity. Additionally, PP1C and SHOC2 do not change conformationally upon the binding of GTP, but rather they are inactive when RAS is bound to GDP due to steric strain. <scene name='95/952694/Pp1coverlay/3'>PP1C retains the same structure</scene> with or without binding to the SMP complex as PP1C retains its enzymatic function independently.<ref name="Liau">PMID: 35768504</ref>.

SHOC2 has a RVxF binding motif that interacts with the PP1C RVxF binding site. The N-terminal loop of SHOC2 interacts with the RVxF binding site of PP1C, highlighting the structure and function connection of the complex. RVxF allows PP1C substrates to bind, whereas RAF has the RVxF motif, so it can bind to the hydrophobic region of SHOC2, allowing for greater specificity. Additionally, PP1C and SHOC2 do not change conformationally upon the binding of GTP, but rather they are inactive when RAS is bound to GDP due to steric strain. <scene name='95/952694/Pp1coverlay/4'>PP1C retains the same structure</scene>with or without binding to the SMP complex as PP1C retains its enzymatic function independently.<ref name="Liau">PMID: 35768504</ref>.

Sandbox Reserved 1766: Difference between revisions

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Revision as of 19:49, 12 April 2023 view source Rosa Trippel (talk \| contribs) 199 edits No edit summary ← Older edit		Revision as of 13:59, 13 April 2023 view source Rosa Trippel (talk \| contribs) 199 edits No edit summary Newer edit →
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	There is a direct interaction between the RVXF motif of SHOC2 and the RVXF-binding pocket of PP1C.<ref name="Hauseman">PMID:35830882</ref>		There is a direct interaction between the RVXF motif of SHOC2 and the RVXF-binding pocket of PP1C.<ref name="Hauseman">PMID:35830882</ref>

	SHOC2 has a RVxF binding motif that interacts with the PP1C RVxF binding site. The N-terminal loop of SHOC2 interacts with the RVxF binding site of PP1C, highlighting the structure and function connection of the complex. RVxF allows PP1C substrates to bind, whereas RAF has the RVxF motif, so it can bind to the hydrophobic region of SHOC2, allowing for greater specificity. Additionally, PP1C and SHOC2 do not change conformationally upon the binding of GTP, but rather they are inactive when RAS is bound to GDP due to steric strain. <scene name='95/952694/Pp1coverlay/3'>PP1C retains the same structure</scene> with or without binding to the SMP complex as PP1C retains its enzymatic function independently.<ref name="Liau">PMID: 35768504</ref>.		SHOC2 has a RVxF binding motif that interacts with the PP1C RVxF binding site. The N-terminal loop of SHOC2 interacts with the RVxF binding site of PP1C, highlighting the structure and function connection of the complex. RVxF allows PP1C substrates to bind, whereas RAF has the RVxF motif, so it can bind to the hydrophobic region of SHOC2, allowing for greater specificity. Additionally, PP1C and SHOC2 do not change conformationally upon the binding of GTP, but rather they are inactive when RAS is bound to GDP due to steric strain. <scene name='95/952694/Pp1coverlay/4'>PP1C retains the same structure</scene>with or without binding to the SMP complex as PP1C retains its enzymatic function independently.<ref name="Liau">PMID: 35768504</ref>.