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==

==Lisinopril==

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''TEMP''=Needs Editing

'''Lisinopril''' (Commercially known as Prinivil) 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.

<ref>Canner, D. Lisinopril http://proteopedia.org/wiki/index.php/prinivil (accessed Nov 10, 2016).</ref>'''Lisinopril''' (Commercially known as Prinivil) 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>. Lisinopril (prinivil) acts upon the membrane protein by forming tight and nonspecific contacts with the conserved residues in the '''S2’,''' '''S1’,''' and '''S1''' positions of the <scene name='74/745974/Lisinopril_ace_complex/2'>ACE</scene><ref>DOI 10.1016/j.jmb.2010.05.024</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.

== Drug Function ==

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== Structure ==

~~== Structure ==~~

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> Lisinopril (prinivil) acts upon the membrane protein by forming tight and nonspecific contacts with the conserved residues in the '''S2’,''' '''S1’,''' and '''S1''' positions of the <scene name='74/745974/Lisinopril_ace_complex/2'>ACE</scene><ref>DOI 10.1016/j.jmb.2010.05.024</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.

== Mechanism ==

Prinivil/Sandbox 1: Difference between revisions

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@@ Line 1: / Line 1: @@
-==<ref>Canner, D. Lisinopril http://proteopedia.org/wiki/index.php/prinivil (accessed Nov 10, 2016).</ref>Lisinopril==
+==Lisinopril==
 <StructureSection load="" size="340" frame="true" spin="on"  scene="74/745974/Lisinopril_stickandball/3" align="right" caption="Lisinopril, commonly known as Prinivil"/>
@@ Line 5: / Line 5: @@
 ''TEMP''=Needs Editing
-'''Lisinopril''' (Commercially known as Prinivil) 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.
+<ref>Canner, D. Lisinopril http://proteopedia.org/wiki/index.php/prinivil (accessed Nov 10, 2016).</ref>'''Lisinopril''' (Commercially known as Prinivil) 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>. Lisinopril (prinivil) acts upon the membrane protein by forming tight and nonspecific contacts with the conserved residues in the '''S2’,''' '''S1’,''' and '''S1''' positions of the <scene name='74/745974/Lisinopril_ace_complex/2'>ACE</scene><ref>DOI 10.1016/j.jmb.2010.05.024</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.
 == Drug Function ==
@@ Line 15: / Line 15: @@
+== Structure ==
-== Structure ==
-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> Lisinopril (prinivil) acts upon the membrane protein by forming tight and nonspecific contacts with the conserved residues in the '''S2’,''' '''S1’,''' and '''S1''' positions of the <scene name='74/745974/Lisinopril_ace_complex/2'>ACE</scene><ref>DOI 10.1016/j.jmb.2010.05.024</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.
 == Mechanism ==