Cocaethylene Synthesis and Pathophysiology: Difference between revisions

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Sarra Borhanian, Michal Harel

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	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/1'>chlorine ion</scene>, and the overall protein is aptly named a glycoprotein due to ligand interactions forming with n-acetyl-d-glucosamine, 2-(acetylamino)-2-deoxy-a-d-glucopyranose, and o-sialic acid		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/2'>chlorine ion</scene>, and the overall protein is aptly named a glycoprotein due to ligand interactions forming with n-acetyl-d-glucosamine, 2-(acetylamino)-2-deoxy-a-d-glucopyranose, and o-sialic acid