The Structure of the NPC1L1 N-Terminal Domain in a Closed Conformation

@inproceedings{Kwon2011TheSO,
  title={The Structure of the NPC1L1 N-Terminal Domain in a Closed Conformation},
  author={Hyock Joo Kwon and Maya Palnitkar and Johann Deisenhofer},
  booktitle={PloS one},
  year={2011}
}
BACKGROUND NPC1L1 is the molecular target of the cholesterol lowering drug Ezetimibe and mediates the intestinal absorption of cholesterol. Inhibition or deletion of NPC1L1 reduces intestinal cholesterol absorption, resulting in reduction of plasma cholesterol levels. PRINCIPAL FINDINGS Here we present the 2.8 Å crystal structure of the N-terminal domain (NTD) of NPC1L1 in the absence of cholesterol. The structure, combined with biochemical data, reveals the mechanism of cholesterol… CONTINUE READING

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Niemann-Pick C1-Like 1 and cholesterol uptake.

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Proceedings of the National Academy of Sciences of the United States of America • 2005
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