Molecular basis of the interactions of the Nogo-66 receptor and its homolog NgR2 with myelin-associated glycoprotein: development of NgROMNI-Fc, a novel antagonist of CNS myelin inhibition.

@article{Robak2009MolecularBO,
  title={Molecular basis of the interactions of the Nogo-66 receptor and its homolog NgR2 with myelin-associated glycoprotein: development of NgROMNI-Fc, a novel antagonist of CNS myelin inhibition.},
  author={Laurie A Robak and Karthik Venkatesh and Hakjoo Lee and Stephen J. Raiker and Yuntao Duan and Jane Lee-Osbourne and Thomas Hofer and Rose G. Mage and Christoph Rader and Roman J Giger},
  journal={The Journal of neuroscience : the official journal of the Society for Neuroscience},
  year={2009},
  volume={29 18},
  pages={5768-83}
}
Myelin-associated glycoprotein (MAG) is a sialic acid-binding Ig-family lectin that functions in neuronal growth inhibition and stabilization of axon-glia interactions. The ectodomain of MAG is comprised of five Ig-like domains and uses neuronal cell-type-specific mechanisms to signal growth inhibition. We show that the first three Ig-like domains of MAG bind with high affinity and in a sialic acid-dependent manner to the Nogo-66 receptor-1 (NgR1) and its homolog NgR2. Domains Ig3-Ig5 of MAG… CONTINUE READING

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