Sandbox 215: Difference between revisions
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==Introduction== | ==Introduction== | ||
[Cholesteryl ester transfer protein http://en.wikipedia.org/wiki/Cholesterylester_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. | [[Cholesteryl ester transfer protein [http://en.wikipedia.org/wiki/Cholesterylester_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 16:10, 24 December 2011
Cholesteryl Ester Transfer Protein (CETP)Cholesteryl Ester Transfer Protein (CETP)
IntroductionIntroduction
[[Cholesteryl ester transfer protein [1]] 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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