The three-dimensional solution structure of the matrix protein from the type D retrovirus, the Mason-Pfizer monkey virus, and implications for the morphology of retroviral assembly.

@article{Conte1997TheTS,
  title={The three-dimensional solution structure of the matrix protein from the type D retrovirus, the Mason-Pfizer monkey virus, and implications for the morphology of retroviral assembly.},
  author={M R Conte and M Klikova and E Hunter and T Ruml and S Matthews},
  journal={The EMBO journal},
  year={1997},
  volume={16 19},
  pages={5819-26}
}
  • M R Conte, M Klikova, +2 authors S Matthews
  • Published 1997 in The EMBO journal
The Mason-Pfizer monkey virus (M-PMV) is the prototype of the type D retroviruses. In type B and D retroviruses, the Gag protein pre-assembles before association with the membrane, whereas in type C retroviruses (lentiviruses, BLV/HTLV group) Gag is targeted efficiently to the plasma membrane, where the particle formation occurs. The N-terminal domain of Gag, the matrix protein (MA), plays a critical role in determining this morphogenic difference. We have determined the three-dimensional… CONTINUE READING
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