Sandbox Reserved 1172: Difference between revisions
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== Structure == | == Structure == | ||
[[Image:Amphbindingfinal.png|200 px|left|thumb|Figure 1: Electrostatic illustration of the amphipathic binding pocket of the LPA<sub>1</sub> 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.]] | [[Image:Amphbindingfinal.png|200 px|left|thumb|Figure 1: Electrostatic illustration of the amphipathic binding pocket of the LPA<sub>1</sub> 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.]] | ||
The LPA<sub>1</sub> receptor protein is composed of 364 amino acids with a molecular weight of approximately 41 kDa. Common to all G-protein coupled receptors, LPA<sub>1</sub> contains seven [http://kinemage.biochem.duke.edu/teaching/anatax/html/anatax.2a.html alpha helices] which make up the seven transmembrane spanning domains with three intracellular loops and three extracellular loops.<ref name = 'Hernández-Méndez'>Hernández-Méndez, Aurelio, Rocío Alcántara-Hernández, and J. Adolfo García-Sáinz. "Lysophosphatidic Acid LPA1-3 Receptors: Signaling, Regulation and in Silico Analysis of Their Putative Phosphorylation Sites." Receptors & Clinical Investigation Receptor Clin Invest 1.3 (2014). Web. 15 Feb. 2016.' </ref>. Within these helices is an amphipathic binding pocket which stabilizes the binding of its ligand, LPA. | The LPA<sub>1</sub> receptor protein is composed of 364 amino acids with a molecular weight of approximately 41 kDa. Common to all G-protein coupled receptors, LPA<sub>1</sub> contains seven [http://kinemage.biochem.duke.edu/teaching/anatax/html/anatax.2a.html alpha helices] which make up the seven transmembrane spanning domains with three intracellular loops and three extracellular loops.<ref name = 'Hernández-Méndez'>Hernández-Méndez, Aurelio, Rocío Alcántara-Hernández, and J. Adolfo García-Sáinz. "Lysophosphatidic Acid LPA1-3 Receptors: Signaling, Regulation and in Silico Analysis of Their Putative Phosphorylation Sites." Receptors & Clinical Investigation Receptor Clin Invest 1.3 (2014). Web. 15 Feb. 2016.' </ref>. Within these helices is an amphipathic binding pocket which stabilizes the binding of its ligand, LPA (Figure 1). | ||
=== Key Ligand Interactions === | === Key Ligand Interactions === | ||
[[Image:Ligandpocket2.png|200 px|right|thumb|Figure 2: Surface representation of the LPA<sub>1</sub> receptor in tan interacting with its antagonist, ON7, shown in green and red sticks.]] | [[Image:Ligandpocket2.png|200 px|right|thumb|Figure 2: Surface representation of the LPA<sub>1</sub> receptor in tan interacting with its antagonist, ON7, shown in green and red sticks.]] | ||
