Cocaethylene Synthesis and Pathophysiology: Difference between revisions

In 2003, a crystal structure of hCE1 was developed using X-ray diffraction techniques to obtain a resolution of 2.80 Angrstoms.  The structure was shown in complex with homatropine, a cocaine analogue, and it comprised of two trimers for a total of six identical subunits.  Each subunit is 548 amino acids long and each is equipped with two catalytic binding sites to process cocaine.  Each trimer subunit associates with a <scene name='Cocaethylene_Synthesis_and_Pathophysiology/Chlorine/3'>chlorine ion</scene>, and the overall protein is aptly named a glycoprotein due to ligand interactions forming with <scene name='Cocaethylene_Synthesis_and_Pathophysiology/N-acetyl-d-glucosamine/1'>n-acetyl-d-glucosamine</scene>, <scene name='Cocaethylene_Synthesis_and_Pathophysiology/2-acetylamino-2-deoxy-a-d-gl/1'>2-(acetylamino)-2-deoxy-a-d-glucopyranose</scene>, and <scene name='Cocaethylene_Synthesis_and_Pathophysiology/O-sialic_acid/1'>o-sialic acid.</scene>