Figure 4: Integrated model of HKU1 S protein trimer with the crystal structure of 1A-S310-677aa. | Nature Communications

Figure 4: Integrated model of HKU1 S protein trimer with the crystal structure of 1A-S310-677aa.

From: Crystal structure of the receptor binding domain of the spike glycoprotein of human betacoronavirus HKU1

Figure 4

(a) The trimeric model of HKU1 S protein with the crystal structure of 1A-S310-677aa. (left) side view; (right) top view. The model is built by superimposing the crystal structure of 1A-S310-677aa into the Cryo-EM structure of the HKU1 S protein trimer18 based on the structure alignment of the core subdomain. The cryo-EM structure of the trimeric HKU1 S protein is shown in grey. The three crystal structures of 1A-S310-677aa are labelled in blue, magenta and green, respectively. The red spheres are sugar moieties found in the crystal structure of 1A-S310-677aa. (b) Superimposition of 1A-S310-677aa onto the cryo-EM density of the HKU1 S protein. The crystal structure of 1A-S310-677aa is shown in blue and the cryo-EM density map is shown in orange. N-linked glycan moieties are shown in red stick.

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