Positive correlation between structural disorder of the HIV-1 Gag N-terminal segment and progeny virus particle formation.

ABSTRACT: A class of unstructured peptide segments termed disordered regions plays a crucial role in the regulation of protein structure and function. Although the N-terminal region of the matrix (MA) domain of the HIV-1 Gag precursor protein is composed of an unstructured peptide, the mechanisms underlying the regulation of the unstructured state relating to control of viral phenotypes remain unclarified. We examined, in association, the structural, evolutionary, and biological roles of the MA N-terminal region via mutagenesis. Molecular dynamics simulation of a full-length Gag dimer model suggested that an amino acid residue at position 9 in the MA N-terminal region (MA-9) participates in the Gag dimerization. Information entropy analysis indicated that the MA-9 residue is variable in nature, but

SUBMITTER: Koma T 

PROVIDER: S-EPMC12548442 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature