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. 2019 May 8;10:2105. doi: 10.1038/s41467-019-09807-5

Fig. 4.

Fig. 4

CR9501 and motavizumab Fabs cannot simultaneously bind to closed, trimeric F. a Monomeric prefusion F-CR9501 structure is shown in ribbons with the F1 subunit colored blue and the F2 subunit colored green. The CR9501 heavy and light chains are shown as dark pink and light pink ribbons, respectively. Motavizumab Fab is modeled onto the prefusion F monomer using the previously solved structure (PDB ID:3IXT) and is shown in ribbons with the heavy and light chains colored orange and tan, respectively. b The two additional protomers of the prefusion F trimer were generated using the C3 symmetry observed in previous crystal structures and are shown as molecular surfaces. c A 90° rotation about the horizontal axis of the complex shown in (b), viewed looking toward the viral membrane. d A second asymmetric unit from the crystal structure, composed of one prefusion F protomer and one CR9501 Fab, and one modeled motavizumab Fab were aligned with a neighboring protomer of the biological trimer and are shown as transparent molecular surfaces. An interprotomeric clash is observed between CR9501 and motavizumab in the context of the prefusion F trimer