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This page, as it appeared on June 14, 2016, was featured in this article in the journal Biochemistry and Molecular Biology Education.

SHOC2-PP1C-MRAS

spinqualitylabelsall models SHOC2-MRAS-PP1C Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Introduction SHOC2-PP1C-MRAS complex is a ternary holophosphatase complex formed by the individual proteins: SHOC2, PP1C, and MRAS. SHOC2-PP1C-MRAS complex is involved in cell proliferation because it functions as a regulator of RTK-RAS signaling by activating RAF through dephosphorization. Complex formation is initiated by ligand binding of receptor tyrosine kinase receptor(RTK). The RTK activates membrane bound MRAS by signaling the exchange of GDP for GTP. GTP bound MRAS initiates complex formation, this complex and is able to dephosphorylate the RAF complex leading to further downstream signaling effects. Overall Structure SHOC2 SHOC2 PP1C PP1C MRAS MRAS Key Ligand Interactions Figure 3: Electrostatic illustration of the amphipathic binding pocket of the LPA1 receptor. This binding pocket was revealed by cutting away the exterior or the protein. This binding pocket, located in the interior of the protein, has both polar and nonpolar regions. The blue and red coloration highlight the positively and negatively charged regions, respectively, and the white color shows the nonpolar region of the binding pocket. 3D structures of lysophosphatidic acid receptor 4z34, 4z35, 4z36 - hLPA1 + antagonist - human 2lq4 – hLPA1 second extracellular loop – NMR 4p0c – hLPA2/NHERF2 5xsz – LPA6A (mutant) – zebra fish Proteopedia Resources Category:Lysophosphatidic acid binding Category:Lysophosphatidic acid Butler University Proteopedia Pages See also: Receptor Transmembrane (cell surface) receptors G protein-coupled receptors

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