Sandbox Reserved 1174: Difference between revisions

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== Structure ==

The LPA1 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 LPA1 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). A cytochrome b (b562RIL) protein was inserted into the third intracellular loop to facilitate crystallization (Figure 2). The intracellular region of this membrane protein is coupled to a [https://www.ebi.ac.uk/interpro/potm/2004_10/Page2.htm heterotrimeric G protein].

The LPA1 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/5'>fatty acid</scene> bound in the crystallization of LPA1 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). A cytochrome b (b562RIL) protein was inserted into the third intracellular loop to facilitate crystallization (Figure 2). The intracellular region of this membrane protein is coupled to a [https://www.ebi.ac.uk/interpro/potm/2004_10/Page2.htm heterotrimeric G protein].

[[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 highlighted in orange.]]

Sandbox Reserved 1174: Difference between revisions

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 == Structure ==
 <StructureSection load='4z34' size='340' side='right' caption=' LPA Receptor 1 ' scene='72/721545/Overall/1'>
-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). A cytochrome b (b<sub>562</sub>RIL) protein was inserted into the third intracellular loop to facilitate crystallization (Figure 2). The intracellular region of this membrane protein is coupled to a [https://www.ebi.ac.uk/interpro/potm/2004_10/Page2.htm heterotrimeric G protein].
+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/5'>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). A cytochrome b (b<sub>562</sub>RIL) protein was inserted into the third intracellular loop to facilitate crystallization (Figure 2). The intracellular region of this membrane protein is coupled to a [https://www.ebi.ac.uk/interpro/potm/2004_10/Page2.htm heterotrimeric G protein].
 [[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 highlighted in orange.]]