Structural and functional studies of ALIX interactions with YPXnL late domains of HIV-1 and EIAV

@article{Zhai2008StructuralAF,
  title={Structural and functional studies of ALIX interactions with YPXnL late domains of HIV-1 and EIAV},
  author={Qianting Zhai and Robert D. Fisher and Hyo-Young Chung and David G. Myszka and Wesley I. Sundquist and Christopher P Hill},
  journal={Nature Structural &Molecular Biology},
  year={2008},
  volume={15},
  pages={43-49}
}
Retrovirus budding requires short peptide motifs (late domains) located within the viral Gag protein that function by recruiting cellular factors. The YPXnL late domains of HIV and other lentiviruses recruit the protein ALIX (also known as AIP1), which also functions in vesicle formation at the multivesicular body and in the abscission stage of cytokinesis. Here, we report the crystal structures of ALIX in complex with the YPXnL late domains from HIV-1 and EIAV. The two distinct late domains… CONTINUE READING