Sandbox Reserved 1160: Difference between revisions

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=== Ionic Locks ===

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.

Another important structural feature is the series of <scene name='72/721531/Ionic_lock/4'>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 24: / Line 24: @@
 === Ionic Locks ===
-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.
+Another important structural feature is the series of <scene name='72/721531/Ionic_lock/4'>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 ==