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Sandbox 47
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(Difference between revisions)
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== '''Structure''' == | == '''Structure''' == | ||
| - | Horse pancreatic lipase (PDB ID 1hpl) consists of 449 amino acids and 705 well-defined water molecules in two subunits, <scene name='Sandbox_47/Lipasechaina/2'>A</scene> and <scene name='Sandbox_47/Lipasechainb/1'>B</scene>. The two chains interact through a variety of <scene name='Sandbox_47/Lipasecontacts/1'>contacts</scene>. 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> and <scene name='Sandbox_47/Lipase_polarres/1'>polar residues</scene>. The overall molecular structure of horse lipase has two well-defined domains. The N-terminal domain contains the <scene name='Sandbox_47/Activesite/ | + | Horse pancreatic lipase (PDB ID 1hpl) consists of 449 amino acids and 705 well-defined water molecules in two subunits, <scene name='Sandbox_47/Lipasechaina/2'>A</scene> and <scene name='Sandbox_47/Lipasechainb/1'>B</scene>. The two chains interact through a variety of <scene name='Sandbox_47/Lipasecontacts/1'>contacts</scene>. 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> and <scene name='Sandbox_47/Lipase_polarres/1'>polar residues</scene>. The overall molecular structure of horse lipase has two well-defined domains. The N-terminal domain 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 that closely resembles that in serine proteases. The C-terminal domain, 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> |
== '''Function''' == | == '''Function''' == | ||
Revision as of 20:25, 12 November 2011
| Please do NOT make changes to this Sandbox. Sandboxes 30-60 are reserved for use by Biochemistry 410 & 412 at Messiah College taught by Dr. Hannah Tims during Fall 2012 and Spring 2013. |
Lipase
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