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'Good cholesterol' structure identified, could help explain protective effects
Date:3/13/2011

rkably similar in structure; however, they found evidence that the particles have a twisting or shock absorber-like motion that allows them to adapt to changes in particle fat content.

By determining the structure of HDL, Davidson and his team were able to conclude that the majority of physiological interactions occurring with HDLincluding its twisting movementsoccur at the particle surface, which is dominated by the cardioprotective protein apolipoprotein A-I.

This monopolization of the particle surface, Davidson says, suggests that other proteins have very little room to bind to HDL and probably have to interact with the protein itself, which could explain how apolipoprotein A-I plays such a dominant role in HDL function and its protective effects.

"This work presents the first detailed models of human plasma HDL and has important implications for understanding key interactions in plasma that modulate its protective functions in the context of cardiovascular disease," says Davidson.


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Contact: Dama Ewbank
dama.ewbank@uc.edu
513-558-4519
University of Cincinnati Academic Health Center
Source:Eurekalert

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