Sandbox 78: Difference between revisions

HGL, a dimeric enzyme consisting of two 379 amino acid residue-long subunits, 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 <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 "lid" 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" />.