Residue Lys57 in the collagen-like region of human L-ficolin and its counterpart Lys47 in H-ficolin play a key role in the interaction with the mannan-binding lectin-associated serine proteases and the collectin receptor calreticulin.

@article{Lacroix2009ResidueLI,
  title={Residue Lys57 in the collagen-like region of human L-ficolin and its counterpart Lys47 in H-ficolin play a key role in the interaction with the mannan-binding lectin-associated serine proteases and the collectin receptor calreticulin.},
  author={Monique Lacroix and C Dumestre-perard and Guy Schoehn and Gunnar Houen and Jean-Yves Cesbron and G{\'e}rard J. Arlaud and Nicole M Thielens},
  journal={Journal of immunology},
  year={2009},
  volume={182 1},
  pages={
          456-65
        }
}
L- and H-ficolins are serum oligomeric defense proteins consisting of a collagen-like region and a fibrinogen-like recognition domain that bind to pathogen- and apoptotic cell-associated molecular patterns. They share with mannan-binding lectin (MBL) the ability to associate with MBL-associated serine proteases (MASP)-1, -2, -3, and protein MAp19 and to trigger the lectin complement pathway through MASP-2 activation. Recent studies have revealed the essential role of Lys(55) in the collagenous… CONTINUE READING

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