Characterization of a putative alpha-helix across the capsid-SP1 boundary that is critical for the multimerization of human immunodeficiency virus type 1 gag.

@article{Liang2002CharacterizationOA,
  title={Characterization of a putative alpha-helix across the capsid-SP1 boundary that is critical for the multimerization of human immunodeficiency virus type 1 gag.},
  author={Chen Liang and Jing Hu and Rodney S Russell and Ariel Rold{\'a}n and Lawrence S. Kleiman and Mark A. Wainberg},
  journal={Journal of virology},
  year={2002},
  volume={76 22},
  pages={11729-37}
}
A 14-amino-acid spacer peptide termed SP1 that separates the capsid (CA) and nucleocapsid (NC) sequences plays an active role in the assembly of human immunodeficiency virus type 1. This activity of SP1 involves its amino-terminal residues that, together with adjacent CA residues, constitute a putative alpha-helical structure spanning Gag residues from positions 359 to 371. In this study, we have determined that the virus assembly determinants within this putative alpha-helix were residues H359… CONTINUE READING