Global structure and dynamics of human apolipoprotein CII in complex with micelles: evidence for increased mobility of the helix involved in the activation of lipoprotein lipase.

@article{Zdunek2003GlobalSA,
  title={Global structure and dynamics of human apolipoprotein CII in complex with micelles: evidence for increased mobility of the helix involved in the activation of lipoprotein lipase.},
  author={Janusz Zdunek and Gary V Martinez and J{\"u}rgen Schleucher and P O Lycksell and Yanxia Yin and Solveig Nilsson and Yan Shen and Gunilla Olivecrona and Sybren Wijmenga},
  journal={Biochemistry},
  year={2003},
  volume={42 7},
  pages={1872-89}
}
Apolipoprotein CII (apoCII), a surface constituent of plasma lipoproteins, is the activator for lipoprotein lipase (LPL) and is therefore central for lipid transport in blood. The three-dimensional structure of (13)C-, (15)N-enriched human full-length apoCII in complex with sodium dodecyl sulfate (SDS) micelles is reported. In addition to the structure… CONTINUE READING