Fig. 3: Structural details of the interaction between E30 and its uncoating (FcRn) or attachment (CD55) receptor. | Nature Communications

Fig. 3: Structural details of the interaction between E30 and its uncoating (FcRn) or attachment (CD55) receptor.

From: Structures of Echovirus 30 in complex with its receptors inform a rational prediction for enterovirus receptor usage

Fig. 3

a Surface representation of E30-FcRn complex (up) and E30-CD55-complex (down) along the icosahedral fivefold axes. The surfaces are colored by radius as shown in the color bar right. b Platform for receptors (FcRn, top and CD5, bottom) binding with E30. The FcRn colored in orange and CD55 colored in magenta are shown in cartoon representation, and viral protomers as surface representation are applied in the same color scheme as in Fig. 1c. c Residues at the main E30-FcRn (up) and E30-CD55 (down) interfaces. The side or main chains involved in mutual interactions are shown as sticks. The hydrogen bonds are shown as yellow dashed lines and the color scheme adopted here is the same as above. d Electrostatic surface representation of E30 and FcRn. The surfaces are colored in a gradient of blue to red in accordance with positive to negative charge, respectively. And the residues in E30 are labeled and circled in the same color in respect to their interacting partners in FcRn. e Roadmap exhibiting the footprints of FcRn (up) or CD55 (down) on the surface of E30. The roadmaps are radius-colored from blue (120 nm) to red (165 nm) with θ and ϕ representing latitude and longitude, respectively. The canyons surrounding the fivefold axes are shaded by shadow. The footprints of FcRn and CD55 are colored in blue and magenta, respectively, and the overlaps between the canyon and FcRn are circled in red lines and accentuated in dark blue.

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