HDL biologyLandmark
A landmark review proposes the first comprehensive step-by-step molecular model of CETP action: sensing, penetration, docking, ternary complex, transfer, dissociation (J Lipid Res 2012)
Original title: New molecular insights into CETP structure and function: a review
Combining new structural and functional methods with prior data on cholesteryl ester transfer protein (CETP), an important clinical drug target whose structure and mechanism of action had not been well understood, this review proposes a detailed multi-step molecular model describing how CETP functions in the context of its interactions with lipoproteins: sensing, penetration, docking, selectivity, ternary complex formation, lipid transfer, and HDL dissociation. By integrating newly available structural data with functional evidence into this stepwise framework, the review provides molecular insights that substantially improve understanding of the mechanisms of action of CETP, establishing a structural and functional reference framework subsequently drawn on across the CETP field.
Original abstract
Cholesteryl ester transfer protein (CETP) is important clinically and is the current target for new drug development. Its structure and mechanism of action has not been well understood. We have combined current new structural and functional methods to compare with relevant prior data. These analyses have led us to propose several steps in CETP's function at the molecular level, in the context of its interactions with lipoproteins, e.g., sensing, penetration, docking, selectivity, ternary complex formation, lipid transfer, and HDL dissociation. These new molecular insights improve our understanding of CETP's mechanisms of action.
Summary written by cetpinhibition.org from the published abstract; figures as published. Page updated 19 August 2026. Methods.