Prinivil/Sandbox 1: Difference between revisions

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''TEMP''=Needs Editing

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 ACE. Then stabilized by ''3 ligands (2 histidine residues and 1 glutamic acid)'' ''Shouldn't these be residues not ligands? Also 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.

'''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 ACE. Then stabilized by ''3 ligands (2 histidine residues and 1 glutamic acid)'' ''Shouldn't these be residues not ligands? Also 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.

== Structure ==

Prinivil/Sandbox 1: Difference between revisions

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@@ Line 6: / Line 6: @@
 ''TEMP''=Needs Editing
-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 ACE. Then stabilized by ''3 ligands (2 histidine residues and 1 glutamic acid)'' ''Shouldn't these be residues not ligands? Also 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.
+'''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 ACE. Then stabilized by ''3 ligands (2 histidine residues and 1 glutamic acid)'' ''Shouldn't these be residues not ligands? Also 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.
 == Structure ==