Sandbox Reserved 1095: Difference between revisions
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=== Primary and secondary structure === | === Primary and secondary structure === | ||
The human AT1 receptor consists of a 376 amino acid string <ref> [http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=4zud&template=main.html Protein Database (PDBsum): 4zud. European Bioinformatics (EBI); 2013.]</ref>. The protein is composed of | The human AT1 receptor consists of a 376 amino acid string <ref> [http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=4zud&template=main.html Protein Database (PDBsum): 4zud. European Bioinformatics (EBI); 2013.]</ref>. The protein is composed of <scene name='82/829348/Helix_a/1'>18 α helixes</scene> and <scene name='82/829348/B_sheet/1'>3 β sheets</scene>. Moreover, 7 α helixes are made of a majority of hydrophobic amino acids. These helixes are long enough to cross the membrane and create a <scene name='82/829348/Transmambrane_protein/1'>hydrophobic domain</scene> which is situated into the membrane. The human angiotensin receptor is therefore an α helical trans-membrane protein. | ||
<scene name='82/829348/Helix_a/1'>18 α | |||
and <scene name='82/829348/B_sheet/1'>3 β sheets</scene>. Moreover, 7 α helixes are made of a majority of hydrophobic amino acids. These helixes are long enough to cross the membrane and create a <scene name='82/829348/Transmambrane_protein/1'>hydrophobic domain</scene> which is situated into the membrane. The human angiotensin receptor is therefore an α helical trans-membrane protein. | |||
Since the angiotensin receptor belongs to the GPCRs family, those 7 α helixes contain 3 extracellular and 3 intracellular loops. The N terminus corresponds to the extracellular domain. The C terminal domain is located intracellularly. | Since the angiotensin receptor belongs to the GPCRs family, those 7 α helixes contain 3 extracellular and 3 intracellular loops. The N terminus corresponds to the extracellular domain. The C terminal domain is located intracellularly. | ||
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=== Interaction with drugs === | === Interaction with drugs === | ||
Angiotensin Receptor Blockers (ARBs) are used to cure diseases linked to AT1R. | Angiotensin Receptor Blockers (ARBs) are used to cure diseases linked to AT1R. | ||
The ARB [https://en.wikipedia.org/wiki/Olmesartan olmesartan] is anchored to ATR1 by the residues <scene name='82/829348/Tyr35/6'>Tyr35</scene>, <scene name='82/829348/Trp84/ | The ARB [https://en.wikipedia.org/wiki/Olmesartan olmesartan] is anchored to ATR1 by the residues <scene name='82/829348/Tyr35/6'>Tyr35</scene>, <scene name='82/829348/Trp84/5'>Trp84</scene> and <scene name='82/829348/Arg167/3'>Arg167</scene>. | ||
Those three amino acids seem to play an important role in the binding of the drug to AT1R, thanks to the formation of extensive networks of hydrogen bonds and salt bridges with the ligand <ref name="Zhang2015"/>. | Those three amino acids seem to play an important role in the binding of the drug to AT1R, thanks to the formation of extensive networks of hydrogen bonds and salt bridges with the ligand <ref name="Zhang2015"/>. | ||