Structural flexibility allows the functional diversity of potyvirus genome-linked protein VPg.

ABSTRACT: Several viral genome-linked proteins (VPgs) of plant viruses are intrinsically disordered and undergo folding transitions in the presence of partners. This property has been postulated to be one of the factors that enable the functional diversity of the protein. We created a homology model of Potato virus A VPg and positioned the known functions and structural properties of potyviral VPgs on the novel structural model. The model suggests an elongated structure with a hydrophobic core composed of antiparallel β-sheets surrounded by helices and a positively charged contact surface where most of the known activities are localized. The model most probably represents the fold induced immediately after binding of VPg to a negatively charged lipid surface or to SDS. When the charge of the positiv

SUBMITTER: Rantalainen KI 

PROVIDER: S-EPMC3067799 | biostudies-literature | 2011 Mar

REPOSITORIES: biostudies-literature