An Intrinsically Disordered Motif Mediates Diverse Actions of Monomeric C-reactive Protein.

@article{Li2016AnID,
  title={An Intrinsically Disordered Motif Mediates Diverse Actions of Monomeric C-reactive Protein.},
  author={Hai-yun Li and Jing Wang and Fan Mei Meng and Zhe-Kun Jia and Yang Yun Su and Qi-Feng Bai and Ling-Ling Lv and Fu-rong Ma and Lawrence Albert Potempa and Yong-Bin Yan and Shang-Rong Ji and Yi Wu},
  journal={The Journal of biological chemistry},
  year={2016},
  volume={291 16},
  pages={
          8795-804
        }
}
Most proinflammatory actions of C-reactive protein (CRP) are only expressed following dissociation of its native pentameric assembly into monomeric form (mCRP). However, little is known about what underlies the greatly enhanced activities of mCRP. Here we show that a single sequence motif, i.e. cholesterol binding sequence (CBS; a.a. 35-47), is responsible for mediating the interactions of mCRP with diverse ligands. The binding of mCRP to lipoprotein component ApoB, to complement component C1q… CONTINUE READING
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