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{{STRUCTURE_2obd|  PDB=2obd  |  SCENE=  }}  
{{STRUCTURE_2obd|  PDB=2obd  |  SCENE=  }}  


[http://en.wikipedia.org/wiki/Cholesterylester_transfer_protein Cholesteryl ester transfer protein (CETP)] belongs to a family of proteins that permits lipid transfer. The [http://en.wikipedia.org/wiki/Homo_sapiens Human] CETP is a hydrophobic glycoprotein which is mainly synthesized in the liver, but also in the intestine, spleen and adrenal glands. The gene coding for this protein is located on the sixteen chromosome.
[http://en.wikipedia.org/wiki/Cholesterylester_transfer_protein Cholesteryl ester transfer protein (CETP)], which is also called plasma lipid transfer protein belongs to a family of proteins that permits lipid transfer. The [http://en.wikipedia.org/wiki/Homo_sapiens human] cholesteryl ester transfer protein  is a hydrophobic glycoprotein which is mainly synthesized in the liver, but also in the intestine, spleen and adrenal glands. The gene coding for this protein is located on the sixteen chromosome.
In the plasma, CETP plays an important role in the transport of cholesteryl esters from the atheroprotective high-density lipoproteins (HDL) to the atherogenic lower-density lipoproteins (LDL) and also mediates the transport of triglycerides from LDL to HDL. Most of the time, CETP facilites homoexchange by exchanging a triglyceride for another triglyceride and a cholesteryl ester for a cholesteryl ester between lipoproteins. However CETP can also promotes heteroexchange.
 
In the plasma, CETP plays an important role in the transport of cholesteryl esters from the atheroprotective high-density lipoproteins (HDL) to the atherogenic lower-density lipoproteins (LDL) and also mediates the transport of triglycerides from LDL to HDL.  
Most of the time, CETP facilites homoexchange by exchanging a triglyceride for another triglyceride and a cholesteryl ester for a cholesteryl ester between lipoproteins. However CETP can also promotes heteroexchange.
The cristal structure of CETP, in complex with four bound lipid molecules at 2,1 Å resolution shows a long tunnel traversing the core of the molecule. This tunnel has two large openings allowing lipids access.  
The cristal structure of CETP, in complex with four bound lipid molecules at 2,1 Å resolution shows a long tunnel traversing the core of the molecule. This tunnel has two large openings allowing lipids access.  


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