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

The binding pocket, as proposed using SCH28080 includes the following residues: Glu936, Lys791, Glu795, Cys813, Cys892, Phe126, and Glu822 (Figure 5). The negatively charged residues within the TM domains are important for K+ binding and are conserved in all P-type ATPases.16 The SCH28080 model shows that electrostatic and hydrophobic factors affect drug-enzyme interaction.16[[Image:pymol.jpg|300px|left|thumb| '''Crystalized Structure of H+/K+-ATPase ''' TM helices 5,6,7,8 are each highlighted in a different color; the majority of the A & B domain within the enzyme, non-catalytic portions of the enzyme, and SCH28080 have been omitted. The figure depicts the proposed binding sites of the crystallized structure of H+/K+-ATPase. Cys813 and Cys892 are highlighted as the two disulfide bond formation sites. Cys 813 is found between TM5 and TM6 domains while Cys892 is between TM7 and TM8 domains.14 Sulfenamide will interact with these two residues and form disulfide bonds. ]][[Image:pymol_2.jpg|300px|right|thumb| '''Binding pocket of SCH28080-ATPase complex''' PDB image obtained from the RCSB Protein Data Bank.15 Image created using PyMol™ Molecular Graphics System. Glu936 (orange), Glu822 (orange), Lys791 (yellow), Glu 795 (orange), Phe126 (gray), Cys892 (light blue), and Cys813 (light blue) are proposed to be part of Esomeprazole’s binding cavity.15,16 ]]

Here is the <scene name='57/571261/Binding_pocket_of_ppis/2'>binding site of Esomeprazole</scene> .