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[http://en.wikipedia.org/wiki/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.
[http://en.wikipedia.org/wiki/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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==Role of CETP==
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==Structure==
<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' />
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==CETP inhibition==
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==References==

Revision as of 13:40, 24 December 2011

Contents

Cholesteryl Ester Transfer Protein (CETP)

PDB ID 2obd

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2obd, resolution 2.10Å ()
Ligands: , , , , , , ,
Gene: CETP (Homo sapiens)
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



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.

Role of CETP

Structure

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CETP inhibition

References

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