Sandbox Reserved 1174: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 9: | Line 9: | ||
Extracellularly, LPA is produced from lysophosphatidylcholine by the enzyme autotaxin.<ref name= "Chrencik"/> Autotaxin was originally linked with metastasis, and this link was later discovered to be mediated through the production of LPA, which signals cell proliferation.<ref name= "Boutin"> DOI: 10.1007/s00018-009-0056-9 </ref> All of LPA’s activities are receptor mediated; the signalling lipid interacts with at least six G-protein coupled receptors LPA<sub>1</sub>-LPA<sub>6</sub>. | Extracellularly, LPA is produced from lysophosphatidylcholine by the enzyme autotaxin.<ref name= "Chrencik"/> Autotaxin was originally linked with metastasis, and this link was later discovered to be mediated through the production of LPA, which signals cell proliferation.<ref name= "Boutin"> DOI: 10.1007/s00018-009-0056-9 </ref> All of LPA’s activities are receptor mediated; the signalling lipid interacts with at least six G-protein coupled receptors LPA<sub>1</sub>-LPA<sub>6</sub>. | ||
| Line 16: | Line 17: | ||
<StructureSection load='4z34' size='340' side='right' caption=' LPA Receptor 1 ' scene='72/721545/Overall/1'> | <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). | ||
[[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.]] | |||
The intracellular region of this membrane protein is coupled to a heterotrimeric G protein. | The intracellular region of this membrane protein is coupled to a heterotrimeric G protein. | ||
=== Structural Stabilization === | === Structural Stabilization === | ||
