Abstract
HIV-1 Gag is a highly flexible multi-domain protein that forms the protein lattice of the immature HIV-1 virion. In vitro it reversibly dimerizes, but in the presence of nucleic acids (NA) it spontaneously assembles into virus-like particles (VLP). While high-resolution structures have revealed intricate detail of the interactions of the capsid domain (CA) of Gag and the flanking spacer peptide SP1 that stabilize VLPs, much less is known about the assembly pathway, and the interactions of the highly flexible NA-binding nucleocapsid (NC) domain.
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