Sandbox 78: Difference between revisions

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== Structural highlights ==

HGL, a 379 amino acid residue-long lipase enzyme, possesses a <scene name='72/728060/Catalytic_elbow/1'>Catalytic Arm</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 <scene name='72/727839/Secondary_structure/1'>Conformation</scene>, where the "lid", residues 215-244 <ref name="dogs">PMID:20965171</ref>, of the lipase gives way to the <scene name='72/728060/Hydrophobic_regions/1'>Hydrophobic Areas</scene> (hydrophobic regions noted in red) 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 <scene name='72/728060/Catalytic_elbow/3'>Catalytic Arm</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 <scene name='72/727839/Secondary_structure/1'>Conformation</scene>, where the "lid", residues 215-244 <ref name="dogs">PMID:20965171</ref>, of the lipase gives way to the <scene name='72/728060/Hydrophobic_regions/1'>Hydrophobic Areas</scene> (hydrophobic regions noted in red) 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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 == Structural highlights ==
-HGL, a 379 amino acid residue-long lipase enzyme, possesses a <scene name='72/728060/Catalytic_elbow/1'>Catalytic Arm</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 <scene name='72/727839/Secondary_structure/1'>Conformation</scene>, where the "lid", residues 215-244 <ref name="dogs">PMID:20965171</ref>, of the lipase gives way to the <scene name='72/728060/Hydrophobic_regions/1'>Hydrophobic Areas</scene> (hydrophobic regions noted in red) 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 <scene name='72/728060/Catalytic_elbow/3'>Catalytic Arm</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 <scene name='72/727839/Secondary_structure/1'>Conformation</scene>, where the "lid", residues 215-244 <ref name="dogs">PMID:20965171</ref>, of the lipase gives way to the <scene name='72/728060/Hydrophobic_regions/1'>Hydrophobic Areas</scene> (hydrophobic regions noted in red) both surrounding the active site and interfacing the lid, thought to draw lipids and promote docking   <ref name="roussel" />.
 == Function ==