Sandbox Reserved 1160: Difference between revisions

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[[Image:STR.png|200 px|left|thumb|'''Figure 1''': Overall Structure of the mGlu5 TMD. The polar heads on the Oliec acids orient the image with the top oriented extracellularly, the middle portion inserted into the membrane, and the lower portion oriented intracellularly. The white exterior represents the surface of the protien, and the multicolored lines interior to the surface represent the backbones 7 transmembrane alpha helices. ]]

=== Overview ===

The mGlu5 TMD contains 7 <scene name='72/721531/Protien_7_helices/4'> alpha helices</scene> that spans the membrane. The protein was crystallized with <scene name='72/721531/Protien_clean_sce/6'>Oleic acid</scene> shown in red. On the top portion of the protein several critical extracellular loops connect the TMD to the CRD. The binding pocket can be found near the middle of the protein, and is mainly comprised of hydrophobic amino acids with more polar amino acids found in the upper and lower portions of the binding site. Inserted into the biding pocket is the negative allosteric modulator [http://www.en.wikipedia.org/wiki/Mavoglurant mavoglurant]. The TMD is in an inactive conformation, since mavoglurant is bound. Also, the deletion of the flexible domains leaves the mGlu5 receptor unable to bind to its [[GPCR]]. The inactive state is maintained by multiple ionic locks whose positions determine the active versus inactive conformation.

The mGlu5 TMD contains 7 <scene name='72/721531/Protien_7_helices/4'> alpha helices</scene> that spans the membrane. The protein was crystallized with <scene name='72/721531/Protien_clean_sce/6'>Oleic acid</scene> shown in '''red'''. On the top portion of the protein several critical extracellular loops connect the TMD to the CRD. The binding pocket can be found near the middle of the protein, and is mainly comprised of hydrophobic amino acids with more polar amino acids found in the upper and lower portions of the binding site. Inserted into the biding pocket is the negative allosteric modulator [http://www.en.wikipedia.org/wiki/Mavoglurant mavoglurant]. The TMD is in an inactive conformation, since mavoglurant is bound. Also, the deletion of the flexible domains leaves the mGlu5 receptor unable to bind to its [[GPCR]]. The inactive state is maintained by multiple ionic locks whose positions determine the active versus inactive conformation.

=== Extracellular Domain ===

These are the <scene name='72/721532/Ecl_trail_7/2'>Extracellular Loops</scene> with extracellular loops (ECLs) 1, 2, and 3 highlighted in purple. Additionally in the ECL domain, a <scene name='72/721531/Ecl_trail_1/5'>disulfide bond</scene> is attached to both Helix 3 and the amino acid chain between Helix 5 and the N-terminus. Helix 3 and Helix 5 are colored in teal and red respectively. N-terminus is represented in blue. The disulfide bond is highlighted in yellow, and it is conserved in all classes of glutamate receptor 5 transmembrane domains<ref name="Wu" /> ECLs and the Helices are also factors that dictate how mavolgarent fits in the binding pocket (citations. The position of these factors can change the size of the binding pocket through tightening or widening.

Sandbox Reserved 1160: Difference between revisions

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@@ Line 11: / Line 11: @@
 [[Image:STR.png|200 px|left|thumb|'''Figure 1''': Overall Structure of the mGlu5 TMD. The polar heads on the Oliec acids orient the image with the top oriented extracellularly, the middle portion inserted into the membrane, and the lower portion oriented intracellularly. The white exterior represents the surface of the protien, and the multicolored lines interior to the surface represent the backbones 7 transmembrane alpha helices. ]]
 === Overview ===
-The mGlu5 TMD contains 7 <scene name='72/721531/Protien_7_helices/4'> alpha helices</scene> that spans the membrane. The protein was crystallized with <scene name='72/721531/Protien_clean_sce/6'>Oleic acid</scene> shown in <font color=''''red''''>red</font>. On the top portion of the protein several critical extracellular loops connect the TMD to the CRD. The binding pocket can be found near the middle of the protein, and is mainly comprised of hydrophobic amino acids with more polar amino acids found in the upper and lower portions of the binding site. Inserted into the biding pocket is the negative allosteric modulator [http://www.en.wikipedia.org/wiki/Mavoglurant mavoglurant]. The TMD is in an inactive conformation, since mavoglurant is bound. Also, the deletion of the flexible domains leaves the mGlu5 receptor unable to bind to its [[GPCR]]. The inactive state is maintained by multiple ionic locks whose positions determine the active versus inactive conformation.
+The mGlu5 TMD contains 7 <scene name='72/721531/Protien_7_helices/4'> alpha helices</scene> that spans the membrane. The protein was crystallized with <scene name='72/721531/Protien_clean_sce/6'>Oleic acid</scene> shown in <font color='red'>'''red'''</font>. On the top portion of the protein several critical extracellular loops connect the TMD to the CRD. The binding pocket can be found near the middle of the protein, and is mainly comprised of hydrophobic amino acids with more polar amino acids found in the upper and lower portions of the binding site. Inserted into the biding pocket is the negative allosteric modulator [http://www.en.wikipedia.org/wiki/Mavoglurant mavoglurant]. The TMD is in an inactive conformation, since mavoglurant is bound. Also, the deletion of the flexible domains leaves the mGlu5 receptor unable to bind to its [[GPCR]]. The inactive state is maintained by multiple ionic locks whose positions determine the active versus inactive conformation.
 === Extracellular Domain ===
 These are the <scene name='72/721532/Ecl_trail_7/2'>Extracellular Loops</scene> with extracellular loops (ECLs) <font color='purple'><b>1</b></font>, <font color='purple'><b>2</b></font>, and <font color='purple'><b>3</b></font> highlighted in <font color='purple'><b>purple</b></font>. Additionally in the ECL domain, a <scene name='72/721531/Ecl_trail_1/5'>disulfide bond</scene> is attached to both Helix 3 and the amino acid chain between Helix 5 and the N-terminus. <font color='teal'><b>Helix 3</b></font> and <font color='red'><b>Helix 5</b></font> are colored in <font color='teal'><b>teal</b></font> and <font color='red'><b>red</b></font> respectively. <font color='blue'><b>N-terminus</b></font> is represented in <font color='blue'><b>blue</b></font>. The <span style="color:yellow;background-color:black;font-weight:bold;">disulfide bond</span> is highlighted in <span style="color:yellow;background-color:black;font-weight:bold;">yellow</span>, and it is conserved in all classes of glutamate receptor 5 transmembrane domains<ref name="Wu" /> ECLs and the Helices are also factors that dictate how mavolgarent fits in the binding pocket (citations. The position of these factors can change the size of the binding pocket through tightening or widening.