Lipase: Difference between revisions
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== '''Inhibition of Pancreatic Lipase''' == | == '''Inhibition of Pancreatic Lipase''' == | ||
In this structure, only one of the two identical chains is shown for lipase and colipase to better visualize the interaction of substrates and ligands with the protein. <scene name='Lipase/Lipase_colipase_inhibitor/1'>Methoxyundecylphosphinic acid (MUP)</scene>, a C11 alkyl phosphonate, is a competitive inhibitor of pancreatic lipase which binds to the active site. It is highlighted in purple. There are also five B-octylglucoside molecules in association with lipase. They are shown in grey and red. MUP forms hydrogen bonds with <scene name='Lipase/Inhibitor_interaction/1'>four residues</scene>: Ser 152 and His 263, which are part of the catalytic triad, and Phe 77 and Leu 153 which are the stabilizing residues located in the oxyanion hole <ref name= "1LPB PDB SUM">[http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=1lpb&template=main.html] 1LPB PDB SUM</ref>. | In this structure, only one of the two identical chains is shown for lipase and colipase to better visualize the interaction of substrates and ligands with the protein. <scene name='Lipase/Lipase_colipase_inhibitor/1'>Methoxyundecylphosphinic acid (MUP)</scene>, a C11 alkyl phosphonate, is a competitive inhibitor of pancreatic lipase which binds to the active site. It is highlighted in purple. There are also five B-octylglucoside molecules in association with lipase. They are shown in grey and red. MUP forms hydrogen bonds with <scene name='Lipase/Inhibitor_interaction/1'>four residues</scene>: Ser 152 and His 263, which are part of the catalytic triad, and Phe 77 and Leu 153 which are the stabilizing residues located in the oxyanion hole <ref name= "1LPB PDB SUM">[http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=1lpb&template=main.html] 1LPB PDB SUM</ref>. | ||
MUP was shown to be <scene name='Sandbox_50/C11p_bound_h_phobics/1'>further stabilized</scene> by van der Waals contacts with hydrophobic side chains Ala 178, Phe 215, Pro l80, Tyr ll4, Leu 213 (shown in blue). | |||
