Fig. 4: EEEV-373 epitope binding footprint on SINV/EEEV particles. | Nature Communications

Fig. 4: EEEV-373 epitope binding footprint on SINV/EEEV particles.

From: Structural elucidation of a unique binding mode by an intact alphavirus human IgG molecule to a quaternary epitope

Fig. 4

A RIVEM (Radial Interpretation of Viral Electron Density Maps) representation of the EEEV-373 IgG binding epitope on the viral surface. Residues within 6 Å of the complementarity-determining regions (CDRs) of EEEV-373 IgG are colored yellow and constitute the epitope binding footprint on the viral surface. The scale bar represents the radial distance in Å from the center of the virus. B Cartoon representation of one arm of the EEEV-373 IgG molecule in complex with a unit of the SINV/EEEV E2/E1 heterodimer. The different protein domains of E1 (domain I: orange, domain II: light pink, domain III: tan), E2 (domain A: cyan, domain B: teal, domain C: aqua, β-ribbon connector: light purple), EEEV-373 heavy chain (green; VH: variable domain, CH1: constant domain), and EEEV-373 light chain (yellow; VL: variable domain, CL: constant domain) are labeled accordingly. C A close-up view of the interface between EEEV-373 and the SINV/EEEV E2/E1 heterodimer. The heavy (green) or light (yellow) chain CDRs 1-3 are indicated as HCDR1, HCDR2, HCDR3 or LCDR1, LCDR2, LCDR3, respectively. The E2 protein domain A (cyan), domain B (teal), β-ribbon connector (light purple), and E1 protein domain II (light pink) are labeled accordingly.

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