Prinivil/Sandbox 1: Difference between revisions
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== Structure == | == Structure == | ||
[[Image:LPR Binding.png|thumb|right|Lisinopril binding locations]]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 S1’ subsite contains '''Glu162''' residue that interacts strongly with the lysine residue of lisinopril, the S1 subsite is surrounded with hydrophobic residues '''Phe512''' and '''Val518''', and the S2’ subsite contains '''Lys511''' and '''Tyr520''' to form strong hydrogen bonds with the C-terminus proline of lisinopril.<ref>DOI 10.1021/ci200083f</ref> | [[Image:LPR Binding.png|thumb|right|Lisinopril binding locations]]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>, which is viewed by using JSmol<ref>DOI 10.1002/ijch.201300024</ref> and Jmol.<ref>PMID:21638687</ref> The S1’ subsite contains '''Glu162''' residue that interacts strongly with the lysine residue of lisinopril, the S1 subsite is surrounded with hydrophobic residues '''Phe512''' and '''Val518''', and the S2’ subsite contains '''Lys511''' and '''Tyr520''' to form strong hydrogen bonds with the C-terminus proline of lisinopril..<ref>DOI 10.1021/ci200083f</ref> | ||
To-do:<br/> | To-do:<br/> | ||
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== References == | == References == | ||
<references/> | <references/> | ||
