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 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].

[[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.]]

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]. When LPA binds in the binding pocket, the G proteins are activated and signal many downstream pathways.

=== Structural Stabilization ===

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The ligand shown in this structure, ONO-9780307, has a similar structure to LPA, and was bound to LPA1 for crystallization to visualize the binding pocket. <ref name= "Moolenaar" /> The <scene name='72/721545/Ligand/2'>binding pocket</scene> for LPA consists of both polar and nonpolar residues. <scene name='72/721545/All_polar_interactions/5'>Polar</scene> residues are located on the N terminus and within the binding pocket (<scene name='72/721545/All_polar_interactions/6'>polar residues</scene>). There is also a <scene name='72/721545/Hydrophobic_pocket/3'>hydrophobic pocket</scene> that interacts with the long acyl chain of LPA.

When LPA binds in the binding pocket, the G protein bound to the intracellular region of LPA1 is activated. This G protein then signals the cell, mainly for survival and proliferation.

=== Sphingosine-1-Phosphate Receptor ===

Sandbox Reserved 1174: Difference between revisions

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@@ Line 16: / Line 16: @@
 == 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 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].
 [[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.]]
-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]. When LPA binds in the binding pocket, the G proteins are activated and signal many downstream pathways.
 === Structural Stabilization ===
@@ Line 29: / Line 27: @@
 The ligand shown in this structure, ONO-9780307, has a similar structure to LPA, and was bound to LPA<sub>1</sub> for crystallization to visualize the binding pocket. <ref name= "Moolenaar" /> The <scene name='72/721545/Ligand/2'>binding pocket</scene> for LPA consists of both polar and nonpolar residues. <scene name='72/721545/All_polar_interactions/5'>Polar</scene> residues are located on the N terminus and within the binding pocket (<scene name='72/721545/All_polar_interactions/6'>polar residues</scene>). There is also a <scene name='72/721545/Hydrophobic_pocket/3'>hydrophobic pocket</scene>  that interacts with the long acyl chain of LPA.
+When LPA binds in the binding pocket, the G protein bound to the intracellular region of LPA<sub>1</sub> is activated. This G protein then signals the cell, mainly for survival and proliferation.
 === Sphingosine-1-Phosphate Receptor ===