User:Alisha, Deepa, Pamiz/Sandbox 1: Difference between revisions

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The interaction between Esomeprazole and H+/K+-ATPase has not yet been crystallized [18]. Data obtained from the crystallized structure of a '''SCH28080-ATPase''' provides structural and binding site information [19]. 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 [19]. 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 [19]. Using this information, the SCH28080-ATPase crystallized structure provides evidence of the two binding sites, Cys813 and Cys892 [18,19]. Cys 813 and Cys 892 residues are within the <scene name='57/571261/Binding_site_of_ppis/2'>binding sites of PPIs</scene>. Here are the <scene name='57/571261/Binding_pocket_of_ppis/2'> residues involved</scene> at the binding pocket of Esomeprazole. Glu936 (green), Glu820 (green), Lys791 (deep red), Glu 795 (green), Phe126 (pink), Cys892 (dark blue), and Cys813 (dark blue) are proposed to be part of Esomeprazole’s binding cavity [18,19].

== Esomeprazole Resistance ==

Revision as of 00:01, 7 December 2013 view source Deepa Patel (talk \| contribs) 230 edits →‎Drug-Molecule Interaction ← Older edit		Revision as of 00:02, 7 December 2013 view source Deepa Patel (talk \| contribs) 230 edits →‎Esomeprazole Resistance Newer edit →
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	The interaction between Esomeprazole and H+/K+-ATPase has not yet been crystallized [18]. Data obtained from the crystallized structure of a '''SCH28080-ATPase''' provides structural and binding site information [19]. 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 [19]. 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 [19]. Using this information, the SCH28080-ATPase crystallized structure provides evidence of the two binding sites, Cys813 and Cys892 [18,19]. Cys 813 and Cys 892 residues are within the <scene name='57/571261/Binding_site_of_ppis/2'>binding sites of PPIs</scene>. Here are the <scene name='57/571261/Binding_pocket_of_ppis/2'> residues involved</scene> at the binding pocket of Esomeprazole. Glu936 (green), Glu820 (green), Lys791 (deep red), Glu 795 (green), Phe126 (pink), Cys892 (dark blue), and Cys813 (dark blue) are proposed to be part of Esomeprazole’s binding cavity [18,19].		The interaction between Esomeprazole and H+/K+-ATPase has not yet been crystallized [18]. Data obtained from the crystallized structure of a '''SCH28080-ATPase''' provides structural and binding site information [19]. 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 [19]. 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 [19]. Using this information, the SCH28080-ATPase crystallized structure provides evidence of the two binding sites, Cys813 and Cys892 [18,19]. Cys 813 and Cys 892 residues are within the <scene name='57/571261/Binding_site_of_ppis/2'>binding sites of PPIs</scene>. Here are the <scene name='57/571261/Binding_pocket_of_ppis/2'> residues involved</scene> at the binding pocket of Esomeprazole. Glu936 (green), Glu820 (green), Lys791 (deep red), Glu 795 (green), Phe126 (pink), Cys892 (dark blue), and Cys813 (dark blue) are proposed to be part of Esomeprazole’s binding cavity [18,19].








	== Esomeprazole Resistance ==		== Esomeprazole Resistance ==