Results: 4

1.
FIG. 1.

FIG. 1. From: Structure of the Nucleoprotein Binding Domain of Mokola Virus Phosphoprotein .

Side-by-side comparison of rhabdovirus P structures: (A) MOKV P; (B) RABV P (PDB accession no. 1VYI); (C) VSV P (PDB accession no. 2K47). The structures are rainbow ramped from blue (N terminus) to red (C terminus).

René Assenberg, et al. J Virol. 2010 January;84(2):1089-1096.
2.
FIG. 4.

FIG. 4. From: Structure of the Nucleoprotein Binding Domain of Mokola Virus Phosphoprotein .

Comparison of the structures of Rhabdovirus and Paramyxovirus N-RNA binding domains of P. (A) Superposition of the conserved elements of MOKV P (orange), VSV P (yellow) (PDB accession no. 2K47), and SeV (magenta) (PDB accession no. 1R4G). Helix numbering is as for MOKV P. The left-hand drawing is based on SHP alignment of the Cα's (40) whereas the right hand drawing is based on the sequence alignment. (B) Side-by-side comparison of the conserved elements of the SeV, MOKV, and VSV P proteins.

René Assenberg, et al. J Virol. 2010 January;84(2):1089-1096.
3.
FIG. 3.

FIG. 3. From: Structure of the Nucleoprotein Binding Domain of Mokola Virus Phosphoprotein .

Mapping the P-N interaction by yeast two-hybrid analysis. Yeast cells expressing Gal4 DNA binding domain (Gal4DB) fused to wild-type PΔ176 (WT) or the indicated mutants were cotransformed with a plasmid encoding the Gal4 transactivation domain (AD) alone (empty vector) or fused to N. Yeast cells were plated on selective medium lacking leucine and tryptophan to validate yeast growth after transformation (−L−W). Selective medium lacking histidine and supplemented with indicated concentrations of 3-aminotriazole (3-AT) were used to test the interaction-dependent transactivation of the HIS3 reporter gene.

René Assenberg, et al. J Virol. 2010 January;84(2):1089-1096.
4.
FIG. 2.

FIG. 2. From: Structure of the Nucleoprotein Binding Domain of Mokola Virus Phosphoprotein .

Details of the major crystal packing interaction interface. (A) View of the interaction between the two neighboring monomers. (B) Close-up of the interactions between the positively charged cluster located on one monomer (green) with the acidic C terminus of the second monomer (yellow). (C) The same view as in panel B but with the green monomer shown as an electrostatic surface representation, generated using the PDB2PQR server (using the AMBER force field [11]) in combination with APBS tools (4) and pymol (http://www.pymol.org/).

René Assenberg, et al. J Virol. 2010 January;84(2):1089-1096.

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