Sandbox Reserved 1174: Difference between revisions

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~~<scene name='72/721545/N-terminus_2/3'>TextToBeDisplayed</scene>~~

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 to it in orange. There are more <scene name='72/721545/Polarity/3'>polar</scene> (red) resides on the intercellular and extracellular areas of the receptor, while most residues positioned 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/2'>fatty acid</scene> bound to it in orange. There are more <scene name='72/721545/Polarity/1'>polar</scene> (red) resides on the intercellular and extracellular areas of the receptor, while most residues positioned inside the membrane are hydrophobic (blue).

[[Image:LPA_in_membrane.fw.png|200px|center|thumb|'''Figure 2:''' LPA in the Phospholipid Bilayer]]

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=== Structural Stabilization ===

There are many different stabilizing factors in the structure of this receptor. There are three native <scene name='72/721545/Disulfides/1'>disulfide bonds</scene> in the extracellular region.<ref name= "Chrencik"/> One of these bonds constrains the N terminal helix to extracellular loop 2. The <scene name='72/721545/N-terminus/1'>N-terminus</scene> functions like a cap on the extracellular side of the protein, packing tightly against ECL1 and ECL2. It also provides <scene name='72/721545/34_39_40/2'>polar amino acids</scene> that interact with the ligand when bound.

There are many different stabilizing factors in the structure of this receptor. There are three native <scene name='72/721545/Disulfides/2'>disulfide bonds</scene> in the extracellular region.<ref name= "Chrencik"/> One of these bonds constrains the N terminal helix to extracellular loop 2. The <scene name='72/721545/N-terminus/2'>N-terminus</scene> functions like a cap on the extracellular side of the protein, packing tightly against ECL1 and ECL2. It also provides <scene name='72/721545/34_39_40/3'>polar amino acids</scene> that interact with the ligand when bound.

=== Binding Pocket ===

Sandbox Reserved 1174: Difference between revisions

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@@ Line 23: / Line 23: @@
 <StructureSection load='4z34' size='340' side='right' caption=' LPA Receptor 1 ' scene='72/721545/Overall/1'>
-<scene name='72/721545/N-terminus_2/3'>TextToBeDisplayed</scene>
+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 to it in orange. There are more <scene name='72/721545/Polarity/3'>polar</scene> (red) resides on the intercellular and extracellular areas of the receptor, while most residues positioned 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/2'>fatty acid</scene> bound to it in orange. There are more <scene name='72/721545/Polarity/1'>polar</scene> (red) resides on the intercellular and extracellular areas of the receptor, while most residues positioned inside the membrane are hydrophobic (blue).
 [[Image:LPA_in_membrane.fw.png|200px|center|thumb|'''Figure 2:''' LPA in the Phospholipid Bilayer]]
@@ Line 31: / Line 29: @@
 === Structural Stabilization ===
-There are many different stabilizing factors in the structure of this receptor. There are three native <scene name='72/721545/Disulfides/1'>disulfide bonds</scene> in the extracellular region.<ref name= "Chrencik"/> One of these bonds constrains the N terminal helix to extracellular loop 2. The <scene name='72/721545/N-terminus/1'>N-terminus</scene> functions like a cap on the extracellular side of the protein, packing tightly against ECL1 and ECL2. It also provides <scene name='72/721545/34_39_40/2'>polar amino acids</scene> that interact with the ligand when bound.
+There are many different stabilizing factors in the structure of this receptor. There are three native <scene name='72/721545/Disulfides/2'>disulfide bonds</scene> in the extracellular region.<ref name= "Chrencik"/> One of these bonds constrains the N terminal helix to extracellular loop 2. The <scene name='72/721545/N-terminus/2'>N-terminus</scene> functions like a cap on the extracellular side of the protein, packing tightly against ECL1 and ECL2. It also provides <scene name='72/721545/34_39_40/3'>polar amino acids</scene> that interact with the ligand when bound.
 === Binding Pocket ===