Sandbox 47: Difference between revisions
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{{Template:Oberholser_Sandbox_Reservation}} | {{Template:Oberholser_Sandbox_Reservation}} | ||
== '''Introduction''' == | == '''Introduction''' == | ||
Pancreatic lipase (EC 3.1.1.3) is an esterase enzyme secreted from the pancreas. It breaks down lipids in the digestive system-converting triglyceride its substrates to monoglycerides and free acids by ester hydrolysis. <ref>"Pancreatic lipase". Wikipedia: The Free Encyclopedia. 7 Nov 2011 [http://en.wikipedia.org/wiki/Pancreatic_lipase]</ref> Pancreatic triglyceride lipase is critical for the efficient absorption of dietary fats.<ref>"Colipase". Wikipedia: The Free Encyclopedia. 5 July 2011 [http://en.wikipedia.org/wiki/Colipase]</ref> | |||
<StructureSection load='1hpl' size='500' frame='true' align='right' scene='Sandbox_47/Liipase/1' caption='Lipase' /> | <StructureSection load='1hpl' size='500' frame='true' align='right' scene='Sandbox_47/Liipase/1' caption='Lipase' /> | ||
== '''Structure''' == | == '''Structure''' == | ||
Horse pancreatic lipase (PDB ID-1hpl) is an asymmetrical molecule that consists of two subunits, each of which contain 449 amino acids and 705 well-defined water molecules. The two subunits, <scene name='Sandbox_47/Lipasechaina/2'>A</scene> and <scene name='Sandbox_47/Lipasechainb/1'>B</scene>, interact through a variety of <scene name='Sandbox_47/Lipasecontacts/1'>contacts</scene>. The subunits are related by a 2-fold non-crystallographic symmetry axis. Lipase also binds two <scene name='Sandbox_47/Lipase_calcium/2'>calcium ions</scene> as ligands through a variety of <scene name='Sandbox_47/Calciumcontacts/4'>contacts</scene>. Its <scene name='Sandbox_47/Lipasesecondarystructures/1'>secondary structure</scene> consists of 22% <scene name='Sandbox_47/Lipase_helix/2'>helices</scene> and 30% <scene name='Sandbox_47/Lipase_sheet/2'>beta sheets</scene>. It contains both <scene name='Sandbox_47/Lipase_hydrophobicres/2'>hydrophobic</scene> (red) and <scene name='Sandbox_47/Lipase_polarres/1'>polar residues</scene> (blue). The overall molecular structure of horse lipase has two well-defined domains. The <scene name='Sandbox_47/Nterminal/1'>N-terminal</scene> domain (residues 1-336) contains the <scene name='Sandbox_47/Activesite/4'>active site</scene> and has a typical alpha/beta hydrolase fold topology. The active site contains a catalytic triad (Ser-152, Asp-176, and His-263) that closely resembles that of serine proteases. The N-terminal domain also contains a <scene name='Sandbox_47/Lid/1'>"lid"</scene> that blocks solvent from entering the active site. The <scene name='Sandbox_47/Cterminal/1'>C-terminal</scene> domain (residues (337-449), for colipase binding, has a beta-sheet sandwich topology.<ref>Bourne Y, Martinez C, Kerfelec B, Lombardo D, Chapus C, Cambillau C. 1994. Horse pancreatic lipase. J. mol Biol. 238: 709-732.</ref> | Horse pancreatic lipase (PDB ID-1hpl) is an asymmetrical molecule that consists of two subunits, each of which contain 449 amino acids and 705 well-defined water molecules. The two subunits, <scene name='Sandbox_47/Lipasechaina/2'>A</scene> and <scene name='Sandbox_47/Lipasechainb/1'>B</scene>, interact through a variety of <scene name='Sandbox_47/Lipasecontacts/1'>contacts</scene>. The subunits are related by a 2-fold non-crystallographic symmetry axis. Lipase also binds two <scene name='Sandbox_47/Lipase_calcium/2'>calcium ions</scene> as ligands through a variety of <scene name='Sandbox_47/Calciumcontacts/4'>contacts</scene>. Its <scene name='Sandbox_47/Lipasesecondarystructures/1'>secondary structure</scene> consists of 22% <scene name='Sandbox_47/Lipase_helix/2'>helices</scene> and 30% <scene name='Sandbox_47/Lipase_sheet/2'>beta sheets</scene>. It contains both <scene name='Sandbox_47/Lipase_hydrophobicres/2'>hydrophobic</scene> (red) and <scene name='Sandbox_47/Lipase_polarres/1'>polar residues</scene> (blue). The overall molecular structure of horse lipase has two well-defined domains. The <scene name='Sandbox_47/Nterminal/1'>N-terminal</scene> domain (residues 1-336) contains the <scene name='Sandbox_47/Activesite/4'>active site</scene> and has a typical alpha/beta hydrolase fold topology. The active site contains a catalytic triad (Ser-152, Asp-176, and His-263) that closely resembles that of serine proteases. The N-terminal domain also contains a <scene name='Sandbox_47/Lid/1'>"lid"</scene> that blocks solvent from entering the active site. The <scene name='Sandbox_47/Cterminal/1'>C-terminal</scene> domain (residues (337-449), for colipase binding, has a beta-sheet sandwich topology.<ref>Bourne Y, Martinez C, Kerfelec B, Lombardo D, Chapus C, Cambillau C. 1994. Horse pancreatic lipase. J. mol Biol. 238: 709-732.</ref> | ||
