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] 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. | ||
Revision as of 13:43, 24 December 2011
Cholesteryl Ester Transfer Protein (CETP)
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| 2obd, resolution 2.10Å (default scene) | |||||||||||||
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| Ligands: | 1PE, 2OB, CL, EPE, PCW, PG4, FU4, NDG | ||||||||||||
| Gene: | CETP (Homo sapiens) | ||||||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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.
