Sandbox 215: Difference between revisions
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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 | [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. | ||