Sandbox Reserved 1095

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=== Recent studies ===
=== Recent studies ===
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Finally, around 2015, researchers have found the crystal structure of the receptor in complex with its antagonist [https://pubchem.ncbi.nlm.nih.gov/compound/ZD-7155-hydrochloride ZD7155] and with an inverse agonist [https://en.wikipedia.org/wiki/Olmesartan olmesartan]<ref name="Zhang2015"> [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4705918/ Zhang H, Unal H, Desnoyer R, et al. Structural Basis for Ligand Recognition and Functional Selectivity at Angiotensin Receptor. J Biol Chem. 2015;290(49):29127–29139. doi:10.1074/jbc.M115.689000] </ref>. [https://en.wikipedia.org/wiki/X-ray_crystallography X-ray cryogenic-crystallography] has been used. They have found similar conformation of the receptor when it is linked to the antagonist or to the inverse agonist. They have also found conserved molecular recognition modes. To complete this discovery, they have realized some experiments with mutants to identify the different residues which interact with the ligand.
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Finally, around 2015, researchers have found the crystal structure of the receptor in complex with its antagonist [https://pubchem.ncbi.nlm.nih.gov/compound/ZD-7155-hydrochloride ZD7155] and with an inverse agonist [https://en.wikipedia.org/wiki/Olmesartan olmesartan]<ref name="Zhang2015"> [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4705918/ Zhang H, Unal H, Desnoyer R, et al. Structural Basis for Ligand Recognition and Functional Selectivity at Angiotensin Receptor. J Biol Chem. 2015;290(49):29127–29139. doi:10.1074/jbc.M115.689000] </ref>. [https://en.wikipedia.org/wiki/X-ray_crystallography X-ray cryogenic-crystallography] has been used. They have found similar conformation of the receptor when it is linked to the antagonist or to the inverse agonist. They have also found conserved molecular recognition modes. To complete this, they have performed mutagenesis experiments and managed to identify several residues in interaction with the ligand.
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The structure of this protein have also been solved using an other method called serial femtosecond crystallography, corresponding to the structure [http://proteopedia.org/wiki/index.php/4yay 4YAY].
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The structure of this protein have also been solved in 2017 using an other method called serial femtosecond crystallography, corresponding to the structure [http://proteopedia.org/wiki/index.php/4yay 4YAY] <ref name="Zhang2017">[Zhang H, Unal H, Gati C, et al. Structure of the Angiotensin receptor revealed by serial femtosecond crystallography. Cell. 2015;161(4):833–844. doi:10.1016/j.cell.2015.04.011 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4427029/]</ref>.
== Structure (function relationship) ==
== Structure (function relationship) ==

Revision as of 14:49, 15 January 2020

This Sandbox is Reserved from 25/11/2019, through 30/9/2020 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1091 through Sandbox Reserved 1115.
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Human Angiotensin Receptor

Angiotensin receptors belong to the G protein coupled receptor (GPCR) family. This is the hormone receptor of the angiotensin II type 1. This is a trans-membrane protein located mainly in heart, brain, liver and kidneys.

Human angiotensin receptor

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References

  1. Angiotensin receptors: History and mysteries, T.L. Goodfriend. American Journal of Hypertension, Volume 13, Issue 4, April 2000, Pages 442–449, https://doi.org/10.1016/S0895-7061(99)00212-5
  2. "Nomenclature for angiotensin receptors. A report of the Nomenclature Committee of the Council for High Blood Pressure Research." Hypertension, 17(5), pp. 720–721.
  3. 3.0 3.1 3.2 Zhang H, Unal H, Desnoyer R, et al. Structural Basis for Ligand Recognition and Functional Selectivity at Angiotensin Receptor. J Biol Chem. 2015;290(49):29127–29139. doi:10.1074/jbc.M115.689000
  4. [Zhang H, Unal H, Gati C, et al. Structure of the Angiotensin receptor revealed by serial femtosecond crystallography. Cell. 2015;161(4):833–844. doi:10.1016/j.cell.2015.04.011 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4427029/]
  5. http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
  6. Fillion D, Cabana J, Guillemette G, Leduc R, Lavigne P, Escher E. Structure of the human angiotensin II type 1 (AT1) receptor bound to angiotensin II from multiple chemoselective photoprobe contacts reveals a unique peptide binding mode. J Biol Chem. 2013;288(12):8187–8197. doi:10.1074/jbc.M112.442053
  7. Singh KD, Unal H, Desnoyer R, Karnik SS. Mechanism of Hormone Peptide Activation of a GPCR: Angiotensin II Activated State of AT1R Initiated by van der Waals Attraction. J Chem Inf Model. 2019;59(1):373–385. doi:10.1021/acs.jcim.8b00583
  8. 8.0 8.1 Takezako T, Unal H, Karnik SS, Node K. Current topics in angiotensin II type 1 receptor research: Focus on inverse agonism, receptor dimerization and biased agonism. Pharmacol Res. 2017;123:40–50. doi:10.1016/j.phrs.2017.06.013
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