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. Author manuscript; available in PMC: 2020 Feb 1.
Published in final edited form as: Antiviral Res. 2018 Dec 11;162:90–100. doi: 10.1016/j.antiviral.2018.12.006

Figure 3. Structural characterization of specific interactions that are important for modulating filoviral replication.

Figure 3.

A. Coiled-coil motif of Reston VP35 N-terminal oligomerization domain arranged as a parallel tetramer (slate; PDB 6GBR). B. Coiled-coil motif of Ebola VP35 N-terminal oligomerization domain arranged as an antiparallel dimer of parallel trimers (molecule A, marine; molecule B, tv blue; PDB 6GBO). C. Ebola VP30 C-terminal domain (warm pink) bound to an Ebola NP peptide (pale green) (PDB 5VAP). D. CDRMs modulating Ebola NP-NP interactions (molecule A, limon; molecule B, split pea; PDB 6C54). E. RNA (yellow) bound Ebola NP (forest) (PDB 5Z9W). F. Ebola NP (chartreuse) bound to an Ebola VP35 peptide NPBP (sky blue) (PDB 4YPI). Structures are colored according to filoviral proteins. Different shades of a color are used to indicate different conformational arrangements. Simple named colors used are defined by PyMOL.