Crystal structure of CD155 and electron microscopic studies of its complexes with polioviruses.

@article{Zhang2008CrystalSO,
  title={Crystal structure of CD155 and electron microscopic studies of its complexes with polioviruses.},
  author={Ping Zhang and Steffen Mueller and Marc C. Morais and Carol M. Bator and Valorie D. Bowman and Susan Hafenstein and Eckard J Wimmer and Michael G. Rossmann},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2008},
  volume={105 47},
  pages={18284-9}
}
When poliovirus (PV) recognizes its receptor, CD155, the virus changes from a 160S to a 135S particle before releasing its genome into the cytoplasm. CD155 is a transmembrane protein with 3 Ig-like extracellular domains, D1-D3, where D1 is recognized by the virus. The crystal structure of D1D2 has been determined to 3.5-A resolution and fitted into approximately 8.5-A resolution cryoelectron microscopy reconstructions of the virus-receptor complexes for the 3 PV serotypes. These structures show… CONTINUE READING
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