Sandbox Reserved 1790: Difference between revisions
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==MRAS== | ==MRAS== | ||
<scene name='95/952717/Mras/2'>MRAS</scene> 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 [https://www.ncbi.nlm.nih.gov/books/NBK442024/. growth factors], the GDP is exchanged for GTP. The now <scene name='95/952718/Zoom_in_gtp/1'>GTP bound MRAS</scene> undergoes a conformational change of the <scene name='95/952716/Ras-switch-zoomed/1'>switch I and switch II regions</scene>. 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 <ref name=”Kubicek”>PMID:11756411</ref>. | <scene name='95/952717/Mras/2'>MRAS</scene> 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 [https://www.ncbi.nlm.nih.gov/books/NBK442024/. growth factors], the GDP is exchanged for GTP. The now <scene name='95/952718/Zoom_in_gtp/1'>GTP bound MRAS</scene> undergoes a conformational change of the <scene name='95/952716/Ras-switch-zoomed/1'>switch I and switch II regions</scene>. 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 <ref name=”Kubicek”>PMID:11756411</ref>. | ||
[[Image:Switches.png|500 px|thumb|'''Figure 2:'''Steric clashing of Switch I and II of GDP bound MRAS, in green, with the surface of SHOC2, in magenta. GTP-bound MRAS, in white, shows no steric clashing with SHOC2s surface.</div></font>]] | |||
=Key Ligand Interactions= | =Key Ligand Interactions= | ||
