Structural basis for collagen recognition by the immune receptor OSCAR.

@article{Zhou2016StructuralBF,
  title={Structural basis for collagen recognition by the immune receptor OSCAR.},
  author={Long Zhou and Jennifer M Hinerman and Michal Blaszczyk and Jeanette L. C. Miller and Deborah G. Conrady and Alexander David Barrow and Dimitri Y. Chirgadze and Dominique G. Bihan and Richard W Farndale and Andrew B Herr},
  journal={Blood},
  year={2016},
  volume={127 5},
  pages={529-37}
}
The osteoclast-associated receptor (OSCAR) is a collagen-binding immune receptor with important roles in dendritic cell maturation and activation of inflammatory monocytes as well as in osteoclastogenesis. The crystal structure of the OSCAR ectodomain is presented, both free and in complex with a consensus triple-helical peptide (THP). The structures revealed a collagen-binding site in each immunoglobulin-like domain (D1 and D2). The THP binds near a predicted collagen-binding groove in D1, but… CONTINUE READING
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Crystal structure and collagen-binding site of immune inhibitory receptor LAIR-1: unexpected implications for collagen binding by platelet receptor GPVI

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