title: Investigation binding patterns of human carboxylesterase I (hCES I) with broad substrates by MD simulations.
abstract: Human carboxylesterase I (hCES 1) plays an important role in the metabolism and activation of prodrugs, such as, the hydrolysis of a variety of drugs of prodrugs featuring an ester, amide or carbamate function. The bindings of the substrates of different lengths and cocaine to hCES1 at two different binding sites, catalytic site and Z-site, were studies through MD simulations. For each case, the correlation analysis has been performed to explore the binding patterns of a broad range of substrates binding to the hCES1.
authors: Laboratory of Molecular Modeling and Design, State key Laboratory of Molecular Reaction Dynamics, Dalian Institute of Chemical Physics, Chinese Academy of Science, 457 Zhongshan Road. Dalian, Liaoning Province, China.
authors: Huiying
authors: H
authors: Chu
authors: Hanyi
authors: H
authors: Min
authors: Mingbo
authors: M
authors: Zhang
authors: Hujun
authors: H
authors: Shen
authors: Guohui
authors: G
authors: Li
mesh_terms: D001665:Binding Sites; D002265:Carboxylic Ester Hydrolases / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D056004:Molecular Dynamics Simulation; D013379:Substrate Specificity
chemical_list: D002265:Carboxylic Ester Hydrolases; C474609:CES1 protein, human