Prinivil/Sandbox 1: Difference between revisions
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<StructureSection load="" size="340" frame="true" spin="on" scene="74/745974/Lisinopril_stickandball/3" align="right" caption="Lisinopril, commonly known as Prinivil"/> | <StructureSection load="" size="340" frame="true" spin="on" scene="74/745974/Lisinopril_stickandball/3" align="right" caption="Lisinopril, commonly known as Prinivil"/> | ||
'''TEMP'''=Green links for structure | '''TEMP'''=Green links for structure<br/> | ||
''TEMP''=Needs Editing | ''TEMP''=Needs Editing | ||
<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. | <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. --> | ||
To-do:<br/> | To-do:<br/> | ||
- | - Patent date<br/> | ||
- More information on clinical trials maybe (?) | |||
== Function == | == Function == | ||
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To-do:<br/> | To-do:<br/> | ||
- other common and relevant ACE inhibitor drugs<br/> | - other common and relevant ACE inhibitor drugs<br/> | ||
- What are diseases in humans that can be helped by lisinopril or affect lisinopril inhibition efficiency. | - What are diseases in humans that can be helped by lisinopril or affect lisinopril inhibition efficiency.<br/> | ||
- More detail on mechanism. Needs more | |||
- Figure out how to use wiki markup in captions of thumbnails if possible (?) | |||
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To-do:<br/> | To-do:<br/> | ||
- Common source of Zn in ACE<br/> | - Common source of Zn in ACE<br/> | ||
- Include Green links for structure viewing of various ACE sites and relevant molecules | - Include Green links for structure viewing of various ACE sites and relevant molecules<br/> | ||
- Create structures for viewing | |||
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- all relevant, interacting residues listed<br/> | - all relevant, interacting residues listed<br/> | ||
- known mechanistic theories<br/> | - known mechanistic theories<br/> | ||
- | - Figure out how to make multiple footnotes referencing the same paper. | ||
=== Robert Sherman, Reef Buckhalter, and Justin Herman all contributed to this article === | |||
(This will be gone in the final edit) | |||
== References == | == References == | ||
<references/> | <references/> | ||
