Sandbox 215: Difference between revisions
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Cholesteryl Ester Transfer Protein (CETP) |
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==Structure== | ==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 owns 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. | |||
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 B-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 B-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 and she interacts with N-terminal residues | |||
