Sandbox Reserved 1172: Difference between revisions
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== Structure == | == Structure == | ||
[[Image:ABP.png|250 px|left|thumb|Electrostatic illustration of the amphipathic binding pocket of the LPA<sub>1</sub> receptor.]] | [[Image:ABP.png|250 px|left|thumb|Electrostatic illustration of the amphipathic binding pocket of the LPA<sub>1</sub> receptor.]] | ||
The LPA<sub>1</sub> receptor protein is composed of 364 amino acids with a mass of approximately 41 kDa. Just as other G-protein coupled receptors, LPA<sub>1</sub> contains seven alpha helices which make up the seven transmembrane spanning domains with three intracellular loops and three extracellular loops. The amino terminus of this protein is located on the extracellular side of the membrane, while the carboxyl terminus is located on the intracellular side of the membrane.<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 mass of approximately 41 kDa. Just as other 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. The amino terminus of this protein is located on the extracellular side of the membrane, while the carboxyl terminus is located on the intracellular side of the membrane.<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. | ||
=== Key Ligand Interactions === | === Key Ligand Interactions === | ||
[[Image:ON7.png|250 px|right|thumb|Overall structure of the LPA<sub>1</sub> receptor in tan interacting with its antagonist, ON7, shown in green and red sticks.]] | [[Image:ON7.png|250 px|right|thumb|Overall structure of the LPA<sub>1</sub> receptor in tan interacting with its antagonist, ON7, shown in green and red sticks.]] | ||
