Conserved structural features in the interaction between retroviral surface and transmembrane glycoproteins?

@article{Schulz1992ConservedSF,
  title={Conserved structural features in the interaction between retroviral surface and transmembrane glycoproteins?},
  author={Thomas F Schulz and B. A. Jameson and L Lopalco and Antonio G Siccardi and Robin A Weiss and John P. Moore},
  journal={AIDS research and human retroviruses},
  year={1992},
  volume={8 9},
  pages={1571-80}
}
Among the retroviruses, the surface (SU) and transmembrane (TM) glycoproteins of lentiviruses are linked exclusively by noncovalent bonds. For some C-type retroviruses, however, a small proportion of the SU proteins has been shown to be linked to their TM proteins by a disulfide bond, with the remainder being noncovalently associated. A region near the carboxyl terminus of the HIV-1 SU glycoprotein has been implicated in contacting the TM glycoprotein. Computer modelling indicates that this… CONTINUE READING

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