User:Alisha, Deepa, Pamiz/Sandbox 1: Difference between revisions
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Deepa Patel (talk | contribs) |
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The interaction between Esomeprazole and H+/K+-ATPase has not yet been crystallized.15 Data obtained from the crystallized structure of a '''SCH28080-ATPase''' provides structural and binding site information.16 SCH28080 is a competitive K+ inhibitor that interacts with the enzyme’s Phe126 residue and prevents disulfide bond formation between Omeprazole and Cys813, suggesting mutually exclusive inhibitions and an overlapping binding site.16 The crystallized structure of SCH28080-ATPase shows the same luminal-open (E2) conformation as Esomeprazole, and is the first and only crystallized evidence of PPI-ATPase binding site and conformational change.16 Using this information, the SCH28080-ATPase crystallized structure provides evidence of the two binding sites, Cys813 and Cys892.15,16 | The interaction between Esomeprazole and H+/K+-ATPase has not yet been crystallized.15 Data obtained from the crystallized structure of a '''SCH28080-ATPase''' provides structural and binding site information.16 SCH28080 is a competitive K+ inhibitor that interacts with the enzyme’s Phe126 residue and prevents disulfide bond formation between Omeprazole and Cys813, suggesting mutually exclusive inhibitions and an overlapping binding site.16 The crystallized structure of SCH28080-ATPase shows the same luminal-open (E2) conformation as Esomeprazole, and is the first and only crystallized evidence of PPI-ATPase binding site and conformational change.16 Using this information, the SCH28080-ATPase crystallized structure provides evidence of the two binding sites, Cys813 and Cys892.15,16 | ||
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Here is the <scene name='57/571261/Binding_pocket_of_ppis/2'>binding site of Esomeprazole</scene> . | Here is the <scene name='57/571261/Binding_pocket_of_ppis/2'>binding site of Esomeprazole</scene> . | ||
== Esomeprazole Resistance == | == Esomeprazole Resistance == | ||