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/Oxyanion_hole/1'>Oxyanion Hole</scene> 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,  <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), 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" />.