Sandbox Reserved 1095: Difference between revisions
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=== G protein-binding site === | === G protein-binding site === | ||
When Angiotensine II bind to the angiotensine receptor in the ligand binding pocket, the conformation of the transmembrane domain change which creat a cytosolic cleft for binding and activating of G proteins. In this cleft we can find several conserved residues which form functional motifs present in all GPCRs <ref> https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6457125/#!po=8.33333 </ref>. | When Angiotensine II bind to the angiotensine receptor in the ligand binding pocket, the conformation of the transmembrane domain change which creat a cytosolic cleft for binding and activating of G proteins. In this cleft we can find several conserved residues which form functional motifs present in all [[GPCRs]] <ref> https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6457125/#!po=8.33333 </ref>. | ||
=== Interaction with drugs === | === Interaction with drugs === | ||
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==== Interaction with other | ==== Interaction with other GPCRs ==== | ||
It has been showed that AT1Rs were also able to bind with other GPCRs to form homo- or heterodimers. Those interactions can modify the sensitivity of the receptor, which leads to different physiological and pathological conditions than the GPCR monomer <ref> http://www.jbc.org/content/290/49/29127 </ref> <ref>https://doi.org/10.1016/j.phrs.2017.06.013 </ref>. | It has been showed that AT1Rs were also able to bind with other GPCRs to form homo- or heterodimers. Those interactions can modify the sensitivity of the receptor, which leads to different physiological and pathological conditions than the GPCR monomer <ref> http://www.jbc.org/content/290/49/29127 </ref> <ref>https://doi.org/10.1016/j.phrs.2017.06.013 </ref>. | ||
