Crystal structure of the multifunctional paramyxovirus hemagglutinin-neuraminidase

@article{Crennell2000CrystalSO,
  title={Crystal structure of the multifunctional paramyxovirus hemagglutinin-neuraminidase},
  author={Susan J Crennell and Toru Takimoto and Allen Portner and Garry L. Taylor},
  journal={Nature Structural Biology},
  year={2000},
  volume={7},
  pages={1068-1074}
}
Paramyxoviruses are the main cause of respiratory disease in children. One of two viral surface glycoproteins, the hemagglutinin-neuraminidase (HN), has several functions in addition to being the major surface antigen that induces neutralizing antibodies. Here we present the crystal structures of Newcastle disease virus HN alone and in complex with either an inhibitor or with the β-anomer of sialic acid. The inhibitor complex reveals a typical neuraminidase active site within a β-propeller fold… CONTINUE READING
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