Structural and Molecular Determinants of Membrane Binding by the HIV-1 Matrix Protein.

@article{Mercredi2016StructuralAM,
  title={Structural and Molecular Determinants of Membrane Binding by the HIV-1 Matrix Protein.},
  author={Peter Y Mercredi and Nadine Bucca and Burk Loeliger and Christy R Gaines and Mansi Mehta and Pallavi Bhargava and Philip R Tedbury and Landry Charlier and Nicolas Floquet and Delphine M. Muriaux and Cyril Favard and Charles R Sanders and Eric O. Freed and Jan Marchant and Michael F Summers},
  journal={Journal of molecular biology},
  year={2016},
  volume={428 8},
  pages={1637-55}
}
Assembly of HIV-1 particles is initiated by the trafficking of viral Gag polyproteins from the cytoplasm to the plasma membrane, where they co-localize and bud to form immature particles. Membrane targeting is mediated by the N-terminally myristoylated matrix (MA) domain of Gag and is dependent on the plasma membrane marker phosphatidylinositol-4,5-bisphosphate [PI(4,5)P2]. Recent studies revealed that PI(4,5)P2 molecules containing truncated acyl chains [tr-PI(4,5)P2] are capable of binding MA… CONTINUE READING