Sandbox Reserved 1174: Difference between revisions

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=== Structural Stabilization ===

Three native <scene name='72/721545/Disulfides/5'>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. These disulfide bonds provide intramolecular stabilization along the extracellular region of the LPA<sub>1</sub> receptor, where the substrate enters into the binding pocket. The <scene name='72/721545/N-terminus/3'>N-terminus</scene> is a six turn alpha helix. It functions like a cap on the extracellular side of the protein, packing tightly against ECL1 and ECL2. The N-terminus helix also provides <scene name='72/721545/34_39_40/4'>polar amino acids</scene> that interact with the ligand when bound.

Three native <scene name='72/721545/Disulfides/5'>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. These disulfide bonds provide intramolecular stabilization along the extracellular region of the LPA<sub>1</sub> receptor, where the substrate enters into the binding pocket. The <scene name='72/721545/N-terminus/3'>N-terminus</scene> is a six turn alpha helix. It functions like a cap on the extracellular side of the protein, packing tightly against ECL1 and ECL2. The N-terminus helix also provides <scene name='72/721545/34_39_40/4'>polar amino acids</scene> that interact with the ligand when bound. The N-terminus in conjunction with extracellular loops 1, 2, and 3 help the correct substrate to bind in the binding pocket.

=== Binding Pocket ===

Sandbox Reserved 1174: Difference between revisions

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@@ Line 22: / Line 22: @@
 === Structural Stabilization ===
-Three native <scene name='72/721545/Disulfides/5'>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. These disulfide bonds provide intramolecular stabilization along the extracellular region of the LPA<sub>1</sub> receptor, where the substrate enters into the binding pocket. The <scene name='72/721545/N-terminus/3'>N-terminus</scene> is a six turn alpha helix. It functions like a cap on the extracellular side of the protein, packing tightly against ECL1 and ECL2. The N-terminus helix also provides <scene name='72/721545/34_39_40/4'>polar amino acids</scene> that interact with the ligand when bound.
+Three native <scene name='72/721545/Disulfides/5'>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. These disulfide bonds provide intramolecular stabilization along the extracellular region of the LPA<sub>1</sub> receptor, where the substrate enters into the binding pocket. The <scene name='72/721545/N-terminus/3'>N-terminus</scene> is a six turn alpha helix. It functions like a cap on the extracellular side of the protein, packing tightly against ECL1 and ECL2. The N-terminus helix also provides <scene name='72/721545/34_39_40/4'>polar amino acids</scene> that interact with the ligand when bound. The N-terminus in conjunction with extracellular loops 1, 2, and 3 help the correct substrate to bind in the binding pocket.
 === Binding Pocket ===