Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation.

@article{Borhani1997CrystalSO,
  title={Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation.},
  author={David W. Borhani and Danise P Rogers and Jeffrey A. Engler and Christie G. Brouillette},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1997},
  volume={94 23},
  pages={12291-6}
}
The structure of truncated human apolipoprotein A-I (apo A-I), the major protein component of high density lipoprotein, has been determined at 4-A resolution. The crystals comprise residues 44-243 (exon 4) of apo A-I, a fragment that binds to lipid similarly to intact apo A-I and that retains the lipid-bound conformation even in the absence of lipid. The molecule consists almost entirely of a pseudo-continuous, amphipathic alpha-helix that is punctuated by kinks at regularly spaced proline… CONTINUE READING
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