Sandbox 78: Difference between revisions

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== Structural highlights ==

HGL, a 379 amino acid residue-long lipase enzyme, possesses a catalytic arm consisting of residues Ser-153, His-353, and Asp-324 essential to the breakdown of lipids, coordinated with an oxyanion hole Leu-67 Gln-154 <ref name="dogs">PMID:20965171</ref>, that serves to stabilize the transition state. Structurally, the human gastric lipase exhibits a complex, coordinated conformation, where the "lid", residues 215-244 <ref name="dogs">PMID:20965171</ref>, of the lipase gives way to the hydrophobic areas both surrounding the active site and interfacing the lid, thought to draw lipids and promote docking <ref name="roussel" />.

HGL, a 379 amino acid residue-long lipase enzyme, possesses a catalytic arm <scene name='72/728060/Catalytic_elbow/1'>TextToBeDisplayed</scene> consisting of residues Ser-153, His-353, and Asp-324 essential to the breakdown of lipids, coordinated with an oxyanion hole Leu-67 Gln-154 <ref name="dogs">PMID:20965171</ref>, that serves to stabilize the transition state. Structurally, the human gastric lipase exhibits a complex, coordinated conformation, where the "lid", residues 215-244 <ref name="dogs">PMID:20965171</ref>, of the lipase gives way to the hydrophobic areas both surrounding the active site and interfacing the lid, thought to draw lipids and promote docking <ref name="roussel" />.

== Function ==

Sandbox 78: Difference between revisions

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-<Structure load='1HLG' size='350' frame='true' align='right' caption='Structure of Human Gastric Lipase (PDB input: 1HLG)' scene='72/728060/Catalytic_elbow/1' />
+<Structure load='1HLG' size='350' frame='true' align='right' caption='Structure of Human Gastric Lipase (PDB input: 1HLG)' />
 <Structure load='1HLG' size='350' frame='true' align='right' caption='Hydrophobic and Hydrophilic Regions of Human Gastric Lipase' scene='72/727839/Hydrophobic_and_polar_regions/1' />
 <Structure load='1HLG' size='350' frame='true' align='right' caption='Secondary Structure of Human Gastric Lipase' scene='72/727839/Secondary_structure/1' />
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 == Structural highlights ==
-HGL, a 379 amino acid residue-long lipase enzyme, possesses a catalytic arm consisting of residues Ser-153, His-353, and Asp-324 essential to the breakdown of lipids, coordinated with an oxyanion hole Leu-67 Gln-154 <ref name="dogs">PMID:20965171</ref>, that serves to stabilize the transition state. Structurally, the human gastric lipase exhibits a complex, coordinated conformation, where the "lid", residues 215-244 <ref name="dogs">PMID:20965171</ref>, of the lipase gives way to the hydrophobic areas both surrounding the active site and interfacing the lid, thought to draw lipids and promote docking   <ref name="roussel" />.
+HGL, a 379 amino acid residue-long lipase enzyme, possesses a catalytic arm <scene name='72/728060/Catalytic_elbow/1'>TextToBeDisplayed</scene> consisting of residues Ser-153, His-353, and Asp-324 essential to the breakdown of lipids, coordinated with an oxyanion hole Leu-67 Gln-154 <ref name="dogs">PMID:20965171</ref>, that serves to stabilize the transition state. Structurally, the human gastric lipase exhibits a complex, coordinated conformation, where the "lid", residues 215-244 <ref name="dogs">PMID:20965171</ref>, of the lipase gives way to the hydrophobic areas both surrounding the active site and interfacing the lid, thought to draw lipids and promote docking   <ref name="roussel" />.
 == Function ==