The Mechanism of CETP Revealed by Electron Microscopy and Molecular Dynamic Simulation

来源 :BITs 2rd Annual World Cancer Congress of Cardiology-2010(201 | 被引量 : 0次 | 上传用户:woyaopojiemimaya
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  Human cholestcryl ester transfer protein (CETP), a hydrophobic glycoprotein (476 amino acids, ~74 kDa), mediates the transfer of cholesteryl ester (CE) from high-density lipoproteins (HDL) to apo-B containing lipoproteins (low density lipoproteins-LDL; very low density lipoproteins-VLDL).The crystal structure of CETP reveals a banana shaped protein consisting of N-and C-terminal β-barrel domains, a central β-sheet, and a ~60-(A)-long hydrophobic cavity.Since CETP deficiency is associated with elevated good-cholesterol (HDL-associated) levels via delayed catabolism, as a rcsult, CETP has become a high interest pharmacological drug target.
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