Sandbox Reserved 1790
From Proteopedia
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<scene name='95/952717/Mras/2'>MRAS</scene> | <scene name='95/952717/Mras/2'>MRAS</scene> | ||
- | + | MRAS is a membrane bound structure that aids the complex in localizing near other structures such as the RAS-RAF-MAPK complex in order to initiate downstream signaling. In its inactive state, MRAS is bound to GDP. When signaled by growth factors, the GDP is exchanged for GTP. The now <scene name='95/952718/Zoom_in_gtp/1'>BTP bound MRAS</scene> undergoes a conformational change of the switch I and switch II regions. This conformational change activates the protein allowing it to bind more easily with the SHOC2-PP1C complex. In comparison to other RAS proteins, MRAS has a greater affinity for the SHOC2-PP1C complex. | |
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- | <scene name='95/952718/Zoom_out/1'>Text To Be Displayed</scene> | ||
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=== Key Ligand Interactions === | === Key Ligand Interactions === | ||
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=== SHOC2 and PP1C === | === SHOC2 and PP1C === | ||
PP1C binds to SHOC2 on its leucine rich region(LRR). Specifically, on two broad surfaces between LRR2 and LRR5 and between LRR7 and LRR11. Five main hydrogen bonds 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_shoc2/1'>SHOC2</scene>. The corresponding patches interact to form a <scene name='95/952718/Acid_base_shoc2pp1c/1'>binary complex</scene>. | PP1C binds to SHOC2 on its leucine rich region(LRR). Specifically, on two broad surfaces between LRR2 and LRR5 and between LRR7 and LRR11. Five main hydrogen bonds 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_shoc2/1'>SHOC2</scene>. The corresponding patches interact to form a <scene name='95/952718/Acid_base_shoc2pp1c/1'>binary complex</scene>. | ||
=== SHOC2 and MRAS === | === 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 changed occur withing the switch I and switch II regions to allow MRAS to interact with SHOC2. These interactions include hydrogen bonds of and pi stacking. The primary hydrogen bonds are R288-Q71 and R177-E47. Pi staking occurs at R104-R83. | ||
=== PP1C and MRAS === | === PP1C and MRAS === | ||
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<references/> | <references/> | ||
- | ==Proteopedia Resources== | ||
- | [http://proteopedia.org/wiki/index.php/Category:Lysophosphatidic_acid_binding Category:Lysophosphatidic acid binding] | ||
- | [http://proteopedia.org/wiki/index.php/Category:Lysophosphatidic_acid Category:Lysophosphatidic acid] | ||
- | [http://proteopedia.org/wiki/index.php/User:R._Jeremy_Johnson/CH462:Biochemistry_II_Butler_University Butler University Proteopedia Pages] | ||
- | See also: | ||
- | *[[Receptor]] | ||
- | *[[Transmembrane (cell surface) receptors]] | ||
- | *[[G protein-coupled receptors]] | ||
- | </StructureSection> | ||
==Student Contributors== | ==Student Contributors== | ||
Madeline Gilbert | Madeline Gilbert |
Revision as of 16:42, 6 April 2023
This page, as it appeared on March 17, 2023, was featured in this article in the journal Biochemistry and Molecular Biology Education.
SHOC2-PP1C-MRAS
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