Sandbox 43
From Proteopedia
(Difference between revisions)
| Line 9: | Line 9: | ||
== '''Structure''' == | == '''Structure''' == | ||
| - | The quaternary structure of horse pancreatic lipase (as featured right) contains two molecules which each contain 449 amino acid residues, 705 water molecules, and 1 calcium ion. These two identical molecules are connected by a two-fold symmetry axis. The <scene name='Sandbox_43/Interactions_between_chains/1'>interactions between the a chain and the b chain</scene> include hydrogen bonds and salt bridges. The secondary structure of lipase is composed of 102 residues that constitute 13 <scene name='Sandbox_43/Alpha_helixes/1'>alpha helices</scene> (22% helical) and 139 residues that constitute 28 <scene name='Sandbox_43/Beta_sheets/3'>beta sheet</scene> strands (30% beta sheets). Lipase is essentially composed of two domains, the <scene name='Sandbox_43/N_terminal/1'>N-terminal domain</scene>, which contains the <scene name='Sandbox_43/Active_site/4'>active site</scene> of lipase (consisting of three residues: Ser-152, Asp-176, and His-263). The N-terminal domain also contains the <scene name='Sandbox_43/Active_site/3'>lid region</scene> (residues 216-239) which serves to block the active site, which is nestled in the <scene name='Sandbox_43/Hydrophobic/2'>hydrophobic regions</scene>, from the solvent. Additionally, the <scene name='Sandbox_43/C_terminal/1'>C-terminal domain</scene> is essential to the binding of lipase with colipase, an important cofactor for the catalysis of lipids. This forms the <scene name='Sandbox_43/Complex_with_colipase/1'>lipase-colipase complex</scene>. | + | The quaternary structure of horse pancreatic lipase (as featured right) contains two molecules which each contain 449 amino acid residues, 705 water molecules, and 1 calcium ion. These two identical molecules are connected by a two-fold symmetry axis. The <scene name='Sandbox_43/Interactions_between_chains/1'>interactions between the a chain and the b chain</scene> include <scene name='Sandbox_43/Hydogen_bonds/1'>hydrogen bonds</scene> and salt bridges. The secondary structure of lipase is composed of 102 residues that constitute 13 <scene name='Sandbox_43/Alpha_helixes/1'>alpha helices</scene> (22% helical) and 139 residues that constitute 28 <scene name='Sandbox_43/Beta_sheets/3'>beta sheet</scene> strands (30% beta sheets). Lipase is essentially composed of two domains, the <scene name='Sandbox_43/N_terminal/1'>N-terminal domain</scene>, which contains the <scene name='Sandbox_43/Active_site/4'>active site</scene> of lipase (consisting of three residues: Ser-152, Asp-176, and His-263). The N-terminal domain also contains the <scene name='Sandbox_43/Active_site/3'>lid region</scene> (residues 216-239) which serves to block the active site, which is nestled in the <scene name='Sandbox_43/Hydrophobic/2'>hydrophobic regions</scene>, from the solvent. Additionally, the <scene name='Sandbox_43/C_terminal/1'>C-terminal domain</scene> is essential to the binding of lipase with colipase, an important cofactor for the catalysis of lipids. This forms the <scene name='Sandbox_43/Complex_with_colipase/1'>lipase-colipase complex</scene>. |
== '''Calcium Ligand''' == | == '''Calcium Ligand''' == | ||
The most prominent ligand involved in the structure of lipase is the <scene name='Sandbox_43/Calcium_ligand/3'>calcium ion</scene>. This ion has been shown to promote the folding of lipase into its active dimer state. As such, the calcium ion is extremely important in forming the lipase-fat complex, necessary for the breakdown of lipids. Studies have shown that an increase in calcium concentration in a lipase catalyzed reaction resulted in an increase in the rate of the reaction. | The most prominent ligand involved in the structure of lipase is the <scene name='Sandbox_43/Calcium_ligand/3'>calcium ion</scene>. This ion has been shown to promote the folding of lipase into its active dimer state. As such, the calcium ion is extremely important in forming the lipase-fat complex, necessary for the breakdown of lipids. Studies have shown that an increase in calcium concentration in a lipase catalyzed reaction resulted in an increase in the rate of the reaction. | ||
Revision as of 21:47, 13 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. |
Horse Pancreatic Lipase
Introduction
| |||||||||||
