User:Giselle Flores/Sandbox 1

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==Structural Overview==
==Structural Overview==
===LPL===
===LPL===
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<scene name='87/877513/Original_scene/1'>LPL</scene> is assumed to only be active as a <scene name='87/877513/Lpl_dimer/5'>tetramer</scene> composed of two LPL-GPIHBP1 heterodimers, however, previous studies have argued that the lipase can be active in its <scene name='87/877513/Original_scene/1'>single heterodimeric form</scene>.<ref name=”Arora”>PMID:31072929</ref><ref name=”Beigneux”>PMID:30850549</ref>The N-terminal domain of lipoprotein lipase is known to consist of an alpha/beta hydrolase domain, which is composed of six alpha helices and ten beta-strands. This domain creates an <scene name='87/877513/Alpha-beta_hydrolase_domain_1/3'>alpha beta hydrolase fold</scene>. The C-terminal domain of lipoprotein lipase is composed of twelve beta strands which form a "<scene name='87/877513/Just_barrel_domain_1/1'>barrel domain</scene>".<ref name=”Arora”>PMID:31072929</ref>
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<scene name='87/877513/Original_scene/1'>LPL</scene> is assumed to only be active as a <scene name='87/877513/Lpl_dimer/5'>tetramer</scene> composed of two LPL-GPIHBP1 heterodimers, however, previous studies have argued that the lipase can be active in its <scene name='87/877513/Original_scene/1'>single heterodimeric form</scene>.<ref name=”Arora”>PMID:31072929</ref><ref name=”Beigneux”>PMID:30850549</ref>The N-terminal domain of lipoprotein lipase is known to consist of an alpha/beta hydrolase domain, which is composed of six alpha helices and ten beta strands. This domain creates an <scene name='87/877513/Alpha-beta_hydrolase_domain_1/3'>alpha beta hydrolase fold</scene>. The C-terminal domain of lipoprotein lipase is composed of twelve beta strands which form a "<scene name='87/877513/Just_barrel_domain_1/1'>barrel domain</scene>".<ref name=”Arora”>PMID:31072929</ref>
=== GPIHBP1 ===
=== GPIHBP1 ===
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=== Lid and Lipid Binding Region ===
=== Lid and Lipid Binding Region ===
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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 dimeric form. <ref name=”Arora”>PMID:31072929</ref> 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.
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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”>PMID:31072929</ref> 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.
[[Image:Inhibiting.png|300 px|right|thumb|The novel inhibitor bound between the lipid-binding region of one LPL and the catalytic site of the other LPL of the tetramer.]]
[[Image:Inhibiting.png|300 px|right|thumb|The novel inhibitor bound between the lipid-binding region of one LPL and the catalytic site of the other LPL of the tetramer.]]
==Mechanism==
==Mechanism==
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<ref name=”Beigneux”>PMID:30850549</ref>
<ref name=”Beigneux”>PMID:30850549</ref>
<ref name=”Mead”>PMID:12483461</ref>
<ref name=”Mead”>PMID:12483461</ref>
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<ref name=”Eckel”>PMID:2648155</ref>
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<ref name=”Eckel”>PMID:2648155</ref>
<ref name=”Francis”>PMID:11905095</ref>
<ref name=”Francis”>PMID:11905095</ref>
<ref name=”Austin”>PMID:9526807</ref>
<ref name=”Austin”>PMID:9526807</ref>

Revision as of 01:40, 28 April 2021

Lipoprotein Lipase coupled with GPIHBP1

Lipoprotein Lipase PDB

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Giselle Flores

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