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.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
