Sandbox Reserved 1095: Difference between revisions
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=== Primary and secondary structure === | === 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 <scene name='82/829348/Helix_a/1'>18 alpha helix</scene> and <scene name='82/829348/B_sheet/1'>3 beta helix</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. | 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/1'>18 alpha helix</scene> and <scene name='82/829348/B_sheet/1'>3 beta helix</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. | Since the angiotensin receptor belongs to the GPCRs family, those 7 alpha helix contain 3 extracellular and 3 intracellular <scene name='82/829348/Arg167/4'>loops</scene>. | ||
=== Ligand binding pocket === | === Ligand binding pocket === | ||
