Synergy and allostery in ligand binding by HIV-1 Nef.

ABSTRACT: The Nef protein of human and simian immunodeficiency viruses boosts viral pathogenicity through its interactions with host cell proteins. By combining the polyvalency of its large unstructured regions with the binding selectivity and strength of its folded core domain, Nef can associate with many different host cell proteins, thereby disrupting their functions. For example, the combination of a linear proline-rich motif and hydrophobic core domain surface allows Nef to bind tightly and specifically to SH3 domains of Src family kinases. We investigated whether the interplay between Nef's flexible regions and its core domain could allosterically influence ligand selection. We found that the flexible regions can associate with the core domain in different ways, producing distinct conformation

SUBMITTER: Aldehaiman A 

PROVIDER: S-EPMC8079166 | biostudies-literature | 2021 Apr

REPOSITORIES: biostudies-literature