Sandbox Reserved 1160: Difference between revisions

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Important Amino Acids<ref name="Dore" />:

*<scene name='72/721531/Protien_bindtop/4'>Asparagine</scene> ~~747forms~~ a hydrogen bond network with the main chain carbonyl of Glycine 652 and the carbamate portion of mavoglurant.

*<scene name='72/721531/Protien_bindtop/4'>Asparagine</scene> 747 forms a hydrogen bond network with the main chain carbonyl of Glycine 652 and the carbamate portion of mavoglurant.

*Bicyclic ring surrounded by <scene name='72/721531/Protien_hydrophobic/1'>hydrophobic binding pocket</scene>.

*2 Catalytic <scene name='72/721531/Protien_bindmiddle/2'>serine</scene> resides H-bond to the hyrdoxyl oxygen of our ligand.

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=== Ionic Locks ===

Another important structural feature is the series of <scene name='72/721531/Ionic_lock/2'>ionic locks</scene> on the intracellular side of the protein. Interactions between amino acids will form a salt bridge, which will stabilize the inactive conformation<ref name="Dore" />. The primary ionic lock forms between Glu770, Lys665, and Ser613<ref name="Dore" />. A secondary ionic lock occurs between Ser614 and Arg668<ref name="Dore" />. The purpose of these ionic locks is analogous to the ionic interactions that stabilize the T state in [[Hemoglobin]]. In the case of the TMD, when the NAM mavoglurant is bound the ionic lock is formed. This stabilizes the inactive state, where the intracellular loops are stabilized inwards<ref name="Wu" />. This will effectively block the crevice that is involved in binding the G-protein<ref name="Wu" />. Models have suggested that, even in a glutamate bound state, the mavoglurant bound receptor would be dimerized but incapable of signaling<ref name="Wu" />. This helps maintain the readiness of the pathway, while still decreasing signal response.

Another important structural feature is the series of <scene name='72/721531/Ionic_lock/3'>ionic locks</scene> on the intracellular side of the protein. Interactions between amino acids will form a salt bridge, which will stabilize the inactive conformation<ref name="Dore" />. The primary ionic lock forms between Glu770, Lys665, and Ser613<ref name="Dore" />. A secondary ionic lock occurs between Ser614 and Arg668<ref name="Dore" />. The purpose of these ionic locks is analogous to the ionic interactions that stabilize the T state in [[Hemoglobin]]. In the case of the TMD, when the NAM mavoglurant is bound the ionic lock is formed. This stabilizes the inactive state, where the intracellular loops are stabilized inwards<ref name="Wu" />. This will effectively block the crevice that is involved in binding the G-protein<ref name="Wu" />. Models have suggested that, even in a glutamate bound state, the mavoglurant bound receptor would be dimerized but incapable of signaling<ref name="Wu" />. This helps maintain the readiness of the pathway, while still decreasing signal response.

== Pathway ==

Sandbox Reserved 1160: Difference between revisions

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@@ Line 16: / Line 16: @@
 Important Amino Acids<ref name="Dore" />:
-*<scene name='72/721531/Protien_bindtop/4'>Asparagine</scene> 747forms a hydrogen bond network with the main chain carbonyl of Glycine 652 and the carbamate portion of mavoglurant.
+*<scene name='72/721531/Protien_bindtop/4'>Asparagine</scene> 747 forms a hydrogen bond network with the main chain carbonyl of Glycine 652 and the carbamate portion of mavoglurant.
 *Bicyclic ring surrounded by <scene name='72/721531/Protien_hydrophobic/1'>hydrophobic binding pocket</scene>.
 *2 Catalytic <scene name='72/721531/Protien_bindmiddle/2'>serine</scene> resides H-bond to the hyrdoxyl oxygen of our ligand.
@@ Line 24: / Line 24: @@
 === Ionic Locks ===
-Another important structural feature is the series of <scene name='72/721531/Ionic_lock/2'>ionic locks</scene> on the intracellular side of the protein. Interactions between amino acids will form a salt bridge, which will stabilize the inactive conformation<ref name="Dore" />. The primary ionic lock forms between Glu770, Lys665, and Ser613<ref name="Dore" />. A secondary ionic lock occurs between Ser614 and Arg668<ref name="Dore" />. The purpose of these ionic locks is analogous to the ionic interactions that stabilize the T state in [[Hemoglobin]]. In the case of the TMD, when the NAM mavoglurant is bound the ionic lock is formed. This stabilizes the inactive state, where the intracellular loops are stabilized inwards<ref name="Wu" />. This will effectively block the crevice that is involved in binding the G-protein<ref name="Wu" />. Models have suggested that, even in a glutamate bound state, the mavoglurant bound receptor would be dimerized but incapable of signaling<ref name="Wu" />. This helps maintain the readiness of the pathway, while still decreasing signal response.
+Another important structural feature is the series of <scene name='72/721531/Ionic_lock/3'>ionic locks</scene> on the intracellular side of the protein. Interactions between amino acids will form a salt bridge, which will stabilize the inactive conformation<ref name="Dore" />. The primary ionic lock forms between Glu770, Lys665, and Ser613<ref name="Dore" />. A secondary ionic lock occurs between Ser614 and Arg668<ref name="Dore" />. The purpose of these ionic locks is analogous to the ionic interactions that stabilize the T state in [[Hemoglobin]]. In the case of the TMD, when the NAM mavoglurant is bound the ionic lock is formed. This stabilizes the inactive state, where the intracellular loops are stabilized inwards<ref name="Wu" />. This will effectively block the crevice that is involved in binding the G-protein<ref name="Wu" />. Models have suggested that, even in a glutamate bound state, the mavoglurant bound receptor would be dimerized but incapable of signaling<ref name="Wu" />. This helps maintain the readiness of the pathway, while still decreasing signal response.
 == Pathway ==