Sandbox Reserved 1715: Difference between revisions

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== Conformational Changes ==

'''1.''' In its resting state, mGlu is in an <scene name='90/904320/Inactive_mglu2_first_picture/6'>inactive homodimeric form</scene>(Figure 3-1). In this conformation, the receptor is considered open with an inter-lobe angle of 44°<ref name="Seven">PMID:34194039</ref>. The structure has two free glutamate binding sites in the VFT, the CRDs are separated, and the TMD is not interacting with a G-protein<ref name="Seven">PMID:34194039</ref>.

'''1.''' In its resting state, mGlu is in an <scene name='90/904320/Inactive_mglu2_first_picture/6'>inactive homodimeric form</scene> (Figure 3-1). In this conformation, the receptor is considered open with an inter-lobe angle of 44°<ref name="Seven">PMID:34194039</ref>. The structure has two free glutamate binding sites in the VFT, the CRDs are separated, and the TMD is not interacting with a G-protein<ref name="Seven">PMID:34194039</ref>.

'''2.''' In the intermediate activation state, also known as the open-closed conformation, one glutamate is bound in one binding pocket of VFT (Figure 3-2). This single <scene name='90/904320/Mglu_binding/9'>glutamate bound state</scene> is still considered inactive as the receptor has not changed the conformations in the CRD and thus the TMD. With the same asymmetric transmembrane helices formation, a <scene name='90/904320/Inactive_tmd_interface/1'>TM3-TM4 interface</scene> is still present and mGlu cannot interact with a G-protein<ref name="Seven">PMID:34194039</ref>.

Sandbox Reserved 1715: Difference between revisions

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@@ Line 45: / Line 45: @@
 == Conformational Changes ==
-'''1.''' In its resting state, mGlu is in an <scene name='90/904320/Inactive_mglu2_first_picture/6'>inactive homodimeric form</scene>(Figure 3-1). In this conformation, the receptor is considered open with an inter-lobe angle of 44°<ref name="Seven">PMID:34194039</ref>. The structure has two free glutamate binding sites in the VFT, the CRDs are separated, and the TMD is not interacting with a G-protein<ref name="Seven">PMID:34194039</ref>.
+'''1.''' In its resting state, mGlu is in an <scene name='90/904320/Inactive_mglu2_first_picture/6'>inactive homodimeric form</scene> (Figure 3-1). In this conformation, the receptor is considered open with an inter-lobe angle of 44°<ref name="Seven">PMID:34194039</ref>. The structure has two free glutamate binding sites in the VFT, the CRDs are separated, and the TMD is not interacting with a G-protein<ref name="Seven">PMID:34194039</ref>.
 '''2.''' In the intermediate activation state, also known as the open-closed conformation, one glutamate is bound in one binding pocket of VFT (Figure 3-2). This single <scene name='90/904320/Mglu_binding/9'>glutamate bound state</scene> is still considered inactive as the receptor has not changed the conformations in the CRD and thus the TMD. With the same asymmetric transmembrane helices formation, a <scene name='90/904320/Inactive_tmd_interface/1'>TM3-TM4 interface</scene> is still present and mGlu cannot interact with a G-protein<ref name="Seven">PMID:34194039</ref>.