Prinivil/Sandbox 1: Difference between revisions

Line 1:

==<ref>Canner, D. Lisinopril http://proteopedia.org/wiki/index.php/prinivil (accessed Nov 10, 2016).</ref>Lisinopril==

~~== Function ==~~

'''TEMP'''=Green links for structure

''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. 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.

'''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 ACE. 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 ==

[[Image:LPR_mechanism.png|left|thumb|Figure 1]]As seen in Figure 1, bradykinin will bind to the ACE, which allows for the conversion of angiotensin I to angiotensis II by theACE/bradykinin complex. By blocking the active site of ACE, an inactive angiostensin 1 cannot be cleaved, which would block the cascade of events triggered by angiotensin 2 binding to type 1 AT2 receptor to create vasoconstriction. ACE is also able to deactivate a common vasodilator known as '''bradykinin''', but when bound to lisinopril, bradykinin levels rise in the blood stream causing a decrease in blood pressure and increased vasodilation.

== Structure ==

<scene name='74/745974/Lisinopril_ace_complex/2'>Lisinopril/ACE Complex</scene>

<scene name='74/745974/Lisinopril_ace_complex/2'>Lisinopril/ACE Complex</scene><ref>DOI 10.1016/j.jmb.2010.05.024</ref>

== Mechanism ==

Prinivil/Sandbox 1: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
 ==<ref>Canner, D. Lisinopril http://proteopedia.org/wiki/index.php/prinivil (accessed Nov 10, 2016).</ref>Lisinopril==
 <StructureSection load="" size="340" frame="true" spin="on"  scene="74/745974/Lisinopril_stickandball/3" align="right" caption="Lisinopril, commonly known as Prinivil"/>
-== Function ==
 '''TEMP'''=Green links for structure
 ''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. 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.
+'''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 ACE. 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 ==
+[[Image:LPR_mechanism.png|left|thumb|Figure 1]]As seen in Figure 1, bradykinin will bind to the ACE, which allows for the conversion of angiotensin I to angiotensis II by theACE/bradykinin complex. By blocking the active site of ACE, an inactive angiostensin 1 cannot be cleaved, which would block the cascade of events triggered by angiotensin 2 binding to type 1 AT2 receptor to create vasoconstriction. ACE is also able to deactivate a common vasodilator known as '''bradykinin''', but when bound to lisinopril, bradykinin levels rise in the blood stream causing a decrease in blood pressure and increased vasodilation.
 == Structure ==
-<scene name='74/745974/Lisinopril_ace_complex/2'>Lisinopril/ACE Complex</scene>
+<scene name='74/745974/Lisinopril_ace_complex/2'>Lisinopril/ACE Complex</scene><ref>DOI 10.1016/j.jmb.2010.05.024</ref>
 == Mechanism ==