Sandbox Reserved 1095: Difference between revisions

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=== Primary and secondary structure ===

Human angiotensin receptor consists in a 376 amino acid string <ref> http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl </ref>. The protein is composed of 18 <scene name='82/829348/Helix_a_and_b_sheet/1'>alpha helix</scene> and 3 <scene name='82/829348/Helix_a_and_b_sheet/1'>beta sheets</scene>. Moreover, 7 alpha helix are made of a majority of hydrophobic amino acids ~~and these~~ helix are long enough to cross the membrane~~. These helix~~ create an <scene name='82/829348/Transmambrane_protein/1'>hydrophobic domain</scene> which is situated into the membrane. The human angiotensin receptor is therefore an alpha helical trans-membrane protein.

Human angiotensin receptor consists in a 376 amino acid string <ref> http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl </ref>. The protein is composed of <scene name='82/829348/Helix_a_and_b_sheet/1'> 18 alpha helix</scene> and <scene name='82/829348/Helix_a_and_b_sheet/1'> 3 beta sheets</scene>. Moreover, 7 alpha helix are made of a majority of hydrophobic amino acids. These helix are long enough to cross the membrane and create an <scene name='82/829348/Transmambrane_protein/1'>hydrophobic domain</scene> which is situated into the membrane. The human angiotensin receptor is therefore an alpha helical trans-membrane protein.

Since the angiotensin receptor belongs to the GPCRs family, those 7 alpha helix contain 3 extracellular and 3 intracellular loops.

=== Ligand binding pocket ===

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=== 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 discovered 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>. The most known heterodimers including AT1 receptor are with ß2-adrenergic receptor, the apelin receptor, and AT2 receptor. Those interactions could be facilitated by several transmembrane domains.

The oligomeric complexes' formation complicates the understanding of AT1R pharmacology.

== Application in the therapeutic field ==

Sandbox Reserved 1095: Difference between revisions

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@@ Line 22: / Line 22: @@
 === Primary and secondary structure ===
-Human angiotensin receptor consists in a 376 amino acid string <ref> http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl </ref>. The protein is composed of 18 <scene name='82/829348/Helix_a_and_b_sheet/1'>alpha helix</scene> and 3 <scene name='82/829348/Helix_a_and_b_sheet/1'>beta sheets</scene>. Moreover, 7 alpha helix are made of a majority of hydrophobic amino acids and these helix are long enough to cross the membrane. These helix create an <scene name='82/829348/Transmambrane_protein/1'>hydrophobic domain</scene> which is situated into the membrane. The human angiotensin receptor is therefore an alpha helical trans-membrane protein.
+Human angiotensin receptor consists in a 376 amino acid string <ref> http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl </ref>. The protein is composed of <scene name='82/829348/Helix_a_and_b_sheet/1'> 18 alpha helix</scene> and <scene name='82/829348/Helix_a_and_b_sheet/1'> 3 beta sheets</scene>. Moreover, 7 alpha helix are made of a majority of hydrophobic amino acids. These helix are long enough to cross the membrane and create an <scene name='82/829348/Transmambrane_protein/1'>hydrophobic domain</scene> which is situated into the membrane. The human angiotensin receptor is therefore an alpha helical trans-membrane protein.
+Since the angiotensin receptor belongs to the GPCRs family, those 7 alpha helix contain 3 extracellular and 3 intracellular loops.
 === Ligand binding pocket ===
@@ Line 42: / Line 43: @@
 === 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 discovered 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>. The most known heterodimers including AT1 receptor are with ß2-adrenergic receptor, the apelin receptor, and AT2 receptor. Those interactions could be facilitated by several transmembrane domains.
+The oligomeric complexes' formation complicates the understanding of AT1R pharmacology.
 == Application in the therapeutic field ==