Research Article

Cauliflower Mosaic Virus TAV, a Plant Virus Protein That Functions like Ribonuclease H1 and is Cytotoxic to Glioma Cells

Figure 1

Modelling the 138-184 domain of CaMV TAV protein. (a) TAV sequence is shown, highlighting (in bold) residues putatively interacting with nucleic acids as predicted with DP-bind. Fragment 138-184 is aligned with the hybrid-binding domain of human RNase H1, whose structure is resolved (PDB: 3BSU) and has been adopted as a template. The alignment of structure-derived and computed secondary structures are also reported. (b) The structure of the double-stranded RNA molecule cocrystallized with the human protein is transferred on the modelled domain upon target-template superimposition. Balls and sticks representation is adopted for the RNA molecule. Residues represented with red Van Der Waals spheres are less than 0.5 nm distant from the RNA molecule. Residue marked ILE 138 is the N-terminus of the modelled domain.
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