Sandbox 43: Difference between revisions

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== '''Structure''' ==

The <scene name='Sandbox_43/Quat_struc/2'>quaternary structure</scene> of horse pancreatic lipase 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 tertiary structure of lipase is stabilized by <scene name='Sandbox_43/Disulfide/1'>disulfide bonds</scene> between cysteine residues. 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, as shown in the N-terminus to C-terminus <scene name='Sandbox_43/N-c_rainbow/1'>rainbow depiction</scene>. The <scene name='Sandbox_43/N_terminal/1'>N-terminal domain</scene>, which contains the <scene name='Sandbox_43/Active_site/8'>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/Hhhhhhhhhhhyrdop/1'>hydrophobic regions</scene>, (in red) from the solvent. Likewise, the active site does not have interactions with the polar, <scene name='Sandbox_43/Hhhhhyrdophilic/1'>hydrophilic regions</scene> (in orange). 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> pictured also with the triglyceride in the substrate binding site.

The <scene name='Sandbox_43/Quat_struc/2'>quaternary structure</scene> of horse pancreatic lipase 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 tertiary structure of lipase is stabilized by <scene name='Sandbox_43/Disulfide/1'>disulfide bonds</scene> between cysteine residues. 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).<ref>http://www.pdb.org/pdb/explore.do?structureId=1HPL</ref> Lipase is essentially composed of two domains, as shown in the N-terminus to C-terminus <scene name='Sandbox_43/N-c_rainbow/1'>rainbow depiction</scene>. The <scene name='Sandbox_43/N_terminal/1'>N-terminal domain</scene>, which contains the <scene name='Sandbox_43/Active_site/8'>active site</scene> of lipase (consisting of three residues: Ser-152, Asp-176, and His-263).<ref>http://www.nature.com/nature/journal/v343/n6260/abs/343771a0.html</ref> 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/Hhhhhhhhhhhyrdop/1'>hydrophobic regions</scene>, (in red) from the solvent. Likewise, the active site does not have interactions with the polar, <scene name='Sandbox_43/Hhhhhyrdophilic/1'>hydrophilic regions</scene> (in orange). 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> pictured also with the triglyceride in the substrate binding site.

== '''Calcium Ligand''' ==

Sandbox 43: Difference between revisions

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 == '''Structure''' ==
-	The <scene name='Sandbox_43/Quat_struc/2'>quaternary structure</scene> of horse pancreatic lipase 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 tertiary structure of lipase is stabilized by <scene name='Sandbox_43/Disulfide/1'>disulfide bonds</scene> between cysteine residues. 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, as shown in the N-terminus to C-terminus <scene name='Sandbox_43/N-c_rainbow/1'>rainbow depiction</scene>. The <scene name='Sandbox_43/N_terminal/1'>N-terminal domain</scene>, which contains the <scene name='Sandbox_43/Active_site/8'>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/Hhhhhhhhhhhyrdop/1'>hydrophobic regions</scene>, (in red) from the solvent. Likewise, the active site does not have interactions with the polar, <scene name='Sandbox_43/Hhhhhyrdophilic/1'>hydrophilic regions</scene> (in orange). 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> pictured also with the triglyceride in the substrate binding site.
+	The <scene name='Sandbox_43/Quat_struc/2'>quaternary structure</scene> of horse pancreatic lipase 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 tertiary structure of lipase is stabilized by <scene name='Sandbox_43/Disulfide/1'>disulfide bonds</scene> between cysteine residues. 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).<ref>http://www.pdb.org/pdb/explore.do?structureId=1HPL</ref> Lipase is essentially composed of two domains, as shown in the N-terminus to C-terminus <scene name='Sandbox_43/N-c_rainbow/1'>rainbow depiction</scene>. The <scene name='Sandbox_43/N_terminal/1'>N-terminal domain</scene>, which contains the <scene name='Sandbox_43/Active_site/8'>active site</scene> of lipase (consisting of three residues: Ser-152, Asp-176, and His-263).<ref>http://www.nature.com/nature/journal/v343/n6260/abs/343771a0.html</ref> 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/Hhhhhhhhhhhyrdop/1'>hydrophobic regions</scene>, (in red) from the solvent. Likewise, the active site does not have interactions with the polar, <scene name='Sandbox_43/Hhhhhyrdophilic/1'>hydrophilic regions</scene> (in orange). 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> pictured also with the triglyceride in the substrate binding site.
 == '''Calcium Ligand''' ==