Sandbox Reserved 1174: Difference between revisions
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== Structure == | == Structure == | ||
<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). | 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). | ||
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Three native <scene name='72/721545/Disulfides/2'>disulfide bonds</scene> in the extracellular region of this receptor provide fold stability.<ref name= "Chrencik"/> The first disulfide bond constrains the N terminal helix to extracellular loop(ECL) 2. The second disulfide bond shapes ECL2, and the third binds ECL3 to one of the transmembrane alpha helices. 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. The N-terminus alpha helix also provides <scene name='72/721545/34_39_40/3'>polar amino acids</scene> that interact with the ligand when bound. | Three native <scene name='72/721545/Disulfides/2'>disulfide bonds</scene> in the extracellular region of this receptor provide fold stability.<ref name= "Chrencik"/> The first disulfide bond constrains the N terminal helix to extracellular loop(ECL) 2. The second disulfide bond shapes ECL2, and the third binds ECL3 to one of the transmembrane alpha helices. 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. The N-terminus alpha helix also provides <scene name='72/721545/34_39_40/3'>polar amino acids</scene> that interact with the ligand when bound. | ||
=== Binding Pocket === | === Binding Pocket === | ||
