Sandbox Reserved 1174: Difference between revisions
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The LPA<sub>1</sub> receptor consists of seven transmembrane alpha helices. It lies in the membrane as shown in Figure 2, and as shown by the <scene name='72/721545/Membrane/4'>fatty acid</scene> bound in the crystallization of LPA<sub>1</sub> in orange. Most <scene name='72/721545/Polarity/3'>polar</scene> (red) reside on the intracellular and extracellular areas of the receptor, while most residues positioned on the trans membrane helices inside the membrane are hydrophobic (blue). | The LPA<sub>1</sub> receptor consists of seven transmembrane alpha helices. It lies in the membrane as shown in Figure 2, and as shown by the <scene name='72/721545/Membrane/4'>fatty acid</scene> bound in the crystallization of LPA<sub>1</sub> in orange. Most <scene name='72/721545/Polarity/3'>polar</scene> (red) reside on the intracellular and extracellular areas of the receptor, while most residues positioned on the trans membrane helices inside the membrane are hydrophobic (blue). | ||
[[Image: | [[Image:LPA_in_membrane4.fw.png|200px|center|thumb|'''Figure 2:''' LPA receptor (blue) bound to the cell membrane. The binding pocket is highlighted in red. The added bRIL protein is shown in orange.]] | ||
=== Structural Stabilization === | === Structural Stabilization === | ||
