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. Author manuscript; available in PMC: 2017 Dec 12.
Published in final edited form as: Nat Biotechnol. 2017 Jun 12;35(7):667–671. doi: 10.1038/nbt.3907

Figure 3. Trimerization of HSB to match the HA trimer.

Figure 3

(a) A co-crystal structure of HSB.2A bound to HK68 HA shows that the design binds to the RBS as designed. (b) Superposition of antibody C05 and the Tri-HSB.2A-HA crystal structure. (c) Close agreement is found for the contacts with HA between the tip of HCDR3 of C05 (blue), the HSB designed model (grey), and the bound crystal structure HSB.2A (orange). (d) Translational and rotational sampling of trimeric protein scaffolds (grey, magenta, blue) to identify trimers that connect the termini of three HSB (orange) molecules bound to trimeric HA (green). Termini of HSB are colored purple and those of the trimerizing unit orange. (e) (top left and middle panels) EM reconstruction of Tri-HSB.1C bound to HK68 HA in side view and top view. (top right and bottom panels) Top view and two side views of the asymmetric EM reconstruction fitted with X-ray structure of HK68 HA bound to HSB.2A monomers; a break in the EM density is indicated by the arrow. (f) BLI titrations of H3 HK68 HA binding to monomeric HSB.2 and trimer Tri-HSB.2.