ATP hydrolysis-dependent conformational changes in the extracellular domain of ABCA1 are associated with apoA-I binding.

@article{Nagao2012ATPHC,
  title={ATP hydrolysis-dependent conformational changes in the extracellular domain of ABCA1 are associated with apoA-I binding.},
  author={Kohjiro Nagao and Kei S Takahashi and Yuya Azuma and Mie Takada and Yasuhisa Kimura and Michinori Matsuo and Noriyuki Kioka and Kazumitsu Ueda},
  journal={Journal of lipid research},
  year={2012},
  volume={53 1},
  pages={126-36}
}
ATP-binding cassette protein A1 (ABCA1) plays a major role in cholesterol homeostasis and high-density lipoprotein (HDL) metabolism. Although it is predicted that apolipoprotein A-I (apoA-I) directly binds to ABCA1, the physiological importance of this interaction is still controversial and the conformation required for apoA-I binding is unclear. In this study, the role of the two nucleotide-binding domains (NBD) of ABCA1 in apoA-I binding was determined by inserting a TEV protease recognition… CONTINUE READING