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 2,2Å 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 | [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 lipids access. | ||
==Role of CETP== | ==Role of CETP== | ||
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CETP's structure can be divided into four structural units: | CETP's structure can be divided into four structural units: | ||
* At each end of the protein there is a barrel which is constitued of highly twisted | * At each end of the protein there is a barrel which is constitued of highly twisted ß-sheet and two helices called A and B at the N-terminal and A', B' at C-terminal extremity. Helices B and B' are longer than A and A' | ||
* Between the two barrels there is a central | * Between the two barrels there is a central ß-sheet which is constitued of six antiparallel strands | ||
* At the C-terminal extremity there is a distorted amphiphathic helix called helix X which is an extension of C-teminal interacting with N-terminal residues. | * At the C-terminal extremity there is a distorted amphiphathic helix called helix X which is an extension of C-teminal interacting with N-terminal residues. | ||