Sandbox Reserved 1095: Difference between revisions

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=== Ligand binding pocket ===
=== Ligand binding pocket ===
In the extracellular environment, there is a β-hairpin in conjugation with <scene name='82/829348/Disulfuric_bridge/1'>two extracellular disulfure bridges</scene>. This structure is responsible for the opening and the locking of the ligand binding pocket <ref> PMID: 23386604  </ref>. The ligand goes into an <scene name='82/829348/Ligand_blinding_pocket/1'>hydrophilic pocket</scene> created into the membrane thanks to the 7 α helix which create a gate between the membrane and the extracellular environment.  
In the extracellular environment, there is a β-hairpin in conjugation with <scene name='82/829348/Disulfuric_bridge/1'>two extracellular disulfure bridges</scene>. This structure is responsible for the opening and the locking of the ligand binding pocket <ref> PMID: 23386604  </ref>. The ligand goes into an <scene name='82/829348/Ligand_blinding_pocket/1'>hydrophilic pocket</scene> created into the membrane thanks to the 7 α helix which create a gate between the membrane and the extracellular environment.
 
=== G protein-binding site ===
 
When the angiotensin II binds to the angiotensin receptor in the ligand binding pocket, the conformation of the trans-membrane domain changes to create a cytosolic cleft for the binding and activation of G proteins. In this cleft, several conserved residues can be found, which form functional motifs present in all [[GPCRs]] <ref> PMID:30608150 </ref>.


AngII mediates AT1 receptor activation via stacking interactions between Phe8(AngII)/<scene name='82/829348/His_256/2'>His256</scene>(AT1 receptor) and Tyr4(AngII)/<scene name='82/829348/Asn_111/1'>Asn111</scene>(AT1 receptor). This phenomenon results in a conformational change in transmembrane (TM)3-TM6 helices and in interaction between TM2 and TM7.  
AngII mediates AT1 receptor activation via stacking interactions between Phe8(AngII)/<scene name='82/829348/His_256/2'>His256</scene>(AT1 receptor) and Tyr4(AngII)/<scene name='82/829348/Asn_111/1'>Asn111</scene>(AT1 receptor). This phenomenon results in a conformational change in transmembrane (TM)3-TM6 helices and in interaction between TM2 and TM7.  
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Many ARBs contain a [https://en.wikipedia.org/wiki/Tetrazole tetrazole] group. Studies showed that tetrazole plays an important role in the binding with AT1R.
Many ARBs contain a [https://en.wikipedia.org/wiki/Tetrazole tetrazole] group. Studies showed that tetrazole plays an important role in the binding with AT1R.
=== G protein-binding site ===
When the angiotensin II binds to the angiotensin receptor in the ligand binding pocket, the conformation of the trans-membrane domain changes to create a cytosolic cleft for the binding and activation of G proteins. In this cleft, several conserved residues can be found, which form functional motifs present in all [[GPCRs]] <ref> PMID:30608150 </ref>.


=== Interaction with other GPCRs ===
=== Interaction with other GPCRs ===
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