Prinivil/Sandbox 1: Difference between revisions
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<ref>Canner, D. Lisinopril http://proteopedia.org/wiki/index.php/prinivil (accessed Nov 10, 2016).</ref>'''Lisinopril''' was patented by Merck & Co. under the brand name of Prinivil.<ref>PRINIVIL® (lisinopril) https://www.merck.com/product/usa/pi_circulars/p/prinivil/prinivil_pi.pdf (accessed Nov 16, 2016).</ref> Lisinopril functions as a competitive inhibitor of the angiotensin converting enzyme (ACE). '''ACE''' cleaves specific residues of an inactive '''angiotensin 1''' near the C domain (domain closer to the C-terminus) to form a potent vasopressor octapeptide known as '''angiotensin 2'''; however the specific substrate binding and catalysis is not fully understood. ACE is found as a type 1 membrane bound dipeptidyl carboxypeptidase that regulates blood pressure and steady state equilibrium of ions within the blood. Located on vascular epithelial cells, the drug interaction takes place on the surface of the cell within an artery/vein.<ref>DOI 10.1038/nature01370</ref>. The ligand is stabilized by ''3 residues (2 histidines (RES #) and 1 glutamic acid (RES #))'' ''We need to add the specific residue bindings here at some point'' interacting through hydrogen bonding along with an ionic binding of a '''Zinc''' atom and the carboxylate group which configures the molecule in 3D space. <!-- There will be a reference here, but can't figure out how to add multiple footnotes for one paper. Need to ask Dr. Berndsen. --> | <ref>Canner, D. Lisinopril http://proteopedia.org/wiki/index.php/prinivil (accessed Nov 10, 2016).</ref>'''Lisinopril''' was patented by Merck & Co. under the brand name of Prinivil.<ref>PRINIVIL® (lisinopril) https://www.merck.com/product/usa/pi_circulars/p/prinivil/prinivil_pi.pdf (accessed Nov 16, 2016).</ref> Lisinopril functions as a competitive inhibitor of the angiotensin converting enzyme (ACE). '''ACE''' cleaves specific residues of an inactive '''angiotensin 1''' near the C domain (domain closer to the C-terminus) to form a potent vasopressor octapeptide known as '''angiotensin 2'''; however, the specific substrate binding and catalysis is not fully understood. ACE is found as a type 1 membrane bound dipeptidyl carboxypeptidase that regulates blood pressure and steady state equilibrium of ions within the blood. Located on vascular epithelial cells, the drug interaction takes place on the surface of the cell within an artery/vein.<ref>DOI 10.1038/nature01370</ref>. The ligand is stabilized by ''3 residues (2 histidines (RES #) and 1 glutamic acid (RES #))'' ''We need to add the specific residue bindings here at some point'' interacting through hydrogen bonding along with an ionic binding of a '''Zinc''' atom and the carboxylate group which configures the molecule in 3D space. <!-- There will be a reference here, but I can't figure out how to add multiple footnotes for one paper. Need to ask Dr. Berndsen. --> | ||
To-do:<br/> | To-do:<br/> | ||
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To-do: | To-do: | ||
- all relevant, interacting residues | - all relevant, interacting residues described<br/> | ||
- known mechanistic theories<br/> | - known mechanistic theories<br/> | ||
- Figure out how to make multiple footnotes referencing the same paper. | - Figure out how to make multiple footnotes referencing the same paper. | ||
