Prinivil/Sandbox 1

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'''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.
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'''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.
== Structure ==
== Structure ==

Revision as of 02:16, 16 November 2016

Contents

[1]Lisinopril

Lisinopril, commonly known as Prinivil

Drag the structure with the mouse to rotate

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.[2] 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.

Structure

Mechanism

Effect in Humans

TEMP

JSmol in Proteopedia [3] or to the article describing Jmol [4] to the re

</StructureSection>

References

  1. ↑ Canner, D. Lisinopril http://proteopedia.org/wiki/index.php/prinivil (accessed Nov 10, 2016).
  2. ↑ Natesh R, Schwager SL, Sturrock ED, Acharya KR. Crystal structure of the human angiotensin-converting enzyme-lisinopril complex. Nature. 2003 Jan 30;421(6922):551-4. Epub 2003 Jan 19. PMID:12540854 doi:http://dx.doi.org/10.1038/nature01370
  3. ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  4. ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644

Proteopedia Page Contributors and Editors (what is this?)

Robert Sherman

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