Sandbox 215: Difference between revisions

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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 traversing 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 2,2Å resolution in complex with four bound lipid molecules shows a long tunnel traversing 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==
==Role of CETP==
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===Overall structure===
===Overall structure===


CETP is a 476 amino acid residues protein which has an elongated “boomerang shape” with dimensions of 135A° X 30 A°X 35A°. She has a molecular mass of 74 kDa and 28% of this mass is attributed to N-glycosylation at specific residues: 88, 240, 341 and 396.
CETP is a 476 amino acid residues protein which has an elongated “boomerang shape” with dimensions of 135Å X 30Å X 35Å. She has a molecular mass of 74 kDa and 28% of this mass is attributed to N-glycosylation at specific residues: 88, 240, 341 and 396.
She also has a fold which is homologous to BPI (a protein which is implicated in lipid binding): two similar domains are connected by a linker.
She also has a fold which is homologous to BPI (a protein which is implicated in lipid binding): two similar domains are connected by a linker.