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

<Structure load='2xzb' size='500' frame='true' align='left' caption='H+/K+-ATPase' scene='Insert optional scene name here' /> 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.