Defective binding of neutral lipids by a carboxyl-terminal deletion mutant of cholesteryl ester transfer protein. Evidence for a carboxyl-terminal cholesteryl ester binding site essential for neutral lipid transfer activity.

@article{Wang1995DefectiveBO,
  title={Defective binding of neutral lipids by a carboxyl-terminal deletion mutant of cholesteryl ester transfer protein. Evidence for a carboxyl-terminal cholesteryl ester binding site essential for neutral lipid transfer activity.},
  author={Shuai Wang and Paul Kussie and L P Deng and Alan Richard Tall},
  journal={The Journal of biological chemistry},
  year={1995},
  volume={270 2},
  pages={612-8}
}
The plasma cholesteryl ester transfer protein (CETP, 476 amino acids) transfers cholesteryl ester (CE) from high density lipoprotein (HDL) to triglyceride-rich lipoproteins and plays a major role in HDL catabolism. Using deletional and site-directed mutagenesis, we previously showed that the carboxyl terminus of human CETP comprises the epitope of a neutralizing monoclonal antibody and is necessary for neutral lipid transfer activity. To assess the nature of the involvement of the COOH terminus… CONTINUE READING
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