Sandbox 78: Difference between revisions

HGL, a dimeric [[hydrolase]] enzyme consisting of two 379 amino acid residue-long subunits, possesses a <scene name='72/728060/Catalytic_elbow/3'>Catalytic Arm</scene> that contains residues Ser-153, His-353, and Asp-324. This structure is essential to the breakdown of lipids, coordinated with an <scene name='72/728060/Arm_and_hole/1'>Oxyanion Hole</scene> at Leu-67 and Gln-154 <ref name="dogs">PMID:20965171</ref>, that serves to stabilize the transition state. Structurally, the human gastric lipase exhibits a complex <scene name='72/728060/Secondary_structure/1'>Secondary Structure</scene> (beta sheets shown in yellow, alpha helices shown in orange, coiled coils shown in green, and amino acid side chains shown as purple). The <scene name='72/728060/1hlg_lid/5'>"Lid"</scene> of the lipase at residues 215-244 <ref name="dogs">PMID:20965171</ref> 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. These areas are thought to draw lipids and promote docking  <ref name="roussel" />.