Sandbox 215
From Proteopedia
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| - | === | + | ===Cholesteryl Ester Transfer Protein (CETP)=== |
==Introduction== | ==Introduction== | ||
| - | [[Cholesteryl ester transfer protein]] is a plasma glycoprotein which is implicated in the transport of cholesteryl esters from the atheroprotective high-density lipoproteins (HDL) to the atherogenic lower-density lipoproteins (LDL). The cristal structure of CETP at 2,2-Å resolution in complex with four bound lipid molecules shows a long tunnel which traverses the core of the molecule and has two distinct large openings allowing lipid access. This tunnel is plugged by an amphiphilic phosphatidylcholine at each end. | + | [Cholesterylester transfer protein[Cholesteryl ester transfer protein]] is a plasma glycoprotein which is implicated in the transport of cholesteryl esters from the atheroprotective high-density lipoproteins (HDL) to the atherogenic lower-density lipoproteins (LDL). The cristal structure of CETP at 2,2-Å resolution in complex with four bound lipid molecules shows a long tunnel which traverses the core of the molecule and has two distinct large openings allowing lipid access. This tunnel is plugged by an amphiphilic phosphatidylcholine at each end. |
<Structure load='2OBD' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | <Structure load='2OBD' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | ||
Revision as of 13:06, 24 December 2011
Cholesteryl Ester Transfer Protein (CETP)
Introduction
[Cholesterylester transfer protein[Cholesteryl ester transfer protein]] is a plasma glycoprotein which is implicated in the transport of cholesteryl esters from the atheroprotective high-density lipoproteins (HDL) to the atherogenic lower-density lipoproteins (LDL). The cristal structure of CETP at 2,2-Å resolution in complex with four bound lipid molecules shows a long tunnel which traverses the core of the molecule and has two distinct large openings allowing lipid access. This tunnel is plugged by an amphiphilic phosphatidylcholine at each end.
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