Fig. 3: The nature of the interactions between CV-A10 and KRM1 shown as open-book views. | Nature Communications

Fig. 3: The nature of the interactions between CV-A10 and KRM1 shown as open-book views.

From: Hand-foot-and-mouth disease virus receptor KREMEN1 binds the canyon of Coxsackie Virus A10

Fig. 3: The nature of the interactions between CV-A10 and KRM1 shown as open-book views.

CV-A10 (a) and KRM1 (b) interface. Both virus and receptor are shown as surface representations. VP1, VP2 and VP3 of CV-A10 are coloured in pale blue, green and red, respectively and an icosahedral subunit outlined with the fivefold (pentamer) and threefold (triangle) symmetry axes labelled, KRM1 from neighbouring subunits are shown in grey with domain names labelled in b. Contact areas between the virus and the receptor with distances ≤4.0 Å are shown in bright red, >4.0 Å and ≤9.0 Å in yellow. The contact areas attributable to two receptors bound at adjacent sites are shown in a. c, d Showing the contact areas on CV-A10 (c) and KRM1 (d) as electrostatic surfaces contoured at ±5 kT e−1 (blue, positive; red, negative) with key residues from the interacting partner shown as sticks with main-chain backbones in orange and sidechains grey in c; residues involved in contacts from the virus capsid VP1, VP2 and VP3 are shown as blue, green and red sticks, respectively in d. e, f Open-book view of electrostatic surfaces of interactions between KRM1 (f) and DKK1 (e). Residues that contact CV-A10 (sticks in e) are also involved in interactions with DKK1 in the KRM1-DKK1-LPR6 complex. DKK1 is shown as ribbons in f.

Back to article page