User:Maggie Stopa/Sandbox 1: Difference between revisions
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=== Calcium Ion Stabilization === | === Calcium Ion Stabilization === | ||
Ions are widely used in proteins and mechanistic stabilization in many areas of biochemistry. LPL’s tertiary folding is stabilized by a Calcium (Ca2+) ion. The calcium ion shares electron density with surrounding residues in order to orient the protein in its formal state.<ref name=”Birrane” /> The <scene name='87/877513/Calcium_stabilization_-labeled/3'>calcium ion stabilization</scene> is achieved by the calcium ion’s interactions with the following of LPL’s residues: Ala194, Arg197, Ser199, Asp201, and Asp202.<ref name=”Birrane” /> | Ions are widely used in proteins and mechanistic stabilization in many areas of biochemistry. LPL’s tertiary folding is stabilized by a Calcium (Ca2+) ion. The calcium ion shares electron density with surrounding residues in order to orient the protein in its formal state.<ref name=”Birrane” /> The <scene name='87/877513/Calcium_stabilization_-labeled/3'>calcium ion stabilization</scene> is achieved by the calcium ion’s interactions with the following of LPL’s residues: Ala194, Arg197, Ser199, Asp201, and Asp202.<ref name=”Birrane” /> | ||
<scene name='87/877513/Lid_region_final/1'>lid region</scene> | |||
=== Lid and Lipid Binding Region === | === Lid and Lipid Binding Region === | ||
In the presence of the GPIHBP1 inhibitor, the <scene name='87/877514/Lid_region_final/1'>lid region</scene> and <scene name='87/877516/Inhibitorsbound/1'>lipid-binding region</scene> become visible within the structure. As displayed through a study conducted by Arora et. al, in 2019, the lipid-binding region of LPL actively interacts with the known inhibitor in the heterodimeric form. <ref name=”Arora” /> This was established to be the only time that the heterodimeric form was shown as an active lipase. The lid region residues Ile245, Ile249, V251, Ile252, Leu257, Val260, Leu263, and Val264, are found as an open conformation which is composed of two small alpha helices that reach out and away from the protein. The lid and lipid-binding region create hydrophobic patches on the surface of lipoprotein lipase which are essential for <scene name='87/877514/Lipid_binding_and_lid/1'>ligand binding</scene> by LPL. | In the presence of the GPIHBP1 inhibitor, the <scene name='87/877514/Lid_region_final/1'>lid region</scene> and <scene name='87/877516/Inhibitorsbound/1'>lipid-binding region</scene> become visible within the structure. As displayed through a study conducted by Arora et. al, in 2019, the lipid-binding region of LPL actively interacts with the known inhibitor in the heterodimeric form. <ref name=”Arora” /> This was established to be the only time that the heterodimeric form was shown as an active lipase. The lid region residues Ile245, Ile249, V251, Ile252, Leu257, Val260, Leu263, and Val264, are found as an open conformation which is composed of two small alpha helices that reach out and away from the protein. The lid and lipid-binding region create hydrophobic patches on the surface of lipoprotein lipase which are essential for <scene name='87/877514/Lipid_binding_and_lid/1'>ligand binding</scene> by LPL. | ||
