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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-MRASSHOC2-PP1C-MRAS

This is a default text for your page Madeline Gilbert/Sandbox 1. Click above on edit this page to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia or to the article describing Jmol to the rescue. Introduction Receptor Tyrosine Kinase Receptor Lipid signaling Transmembrane (cell surface) receptors Figure 1: LPA receptor (blue) bound to the cell membrane. The binding pocket is highlighted in red. The added bRIL protein is highlighted in orange. Lysophosphatidic Acid Figure 2: Chemical Structure of LPA (monoacyl-sn-glycero-3-phosphate) Overall Structure 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

spinqualitylabelsall models SHOC2-MRAS-PP1C Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Student ContributorsStudent Contributors

Madeline Gilbert Inaya Patel Rushda Hussein