Extended Data Fig. 2: Comparison of our apo HKU1-A spike structure with previously published structures and visualisation of its glycan shield.
From: Sialoglycan binding triggers spike opening in a human coronavirus
a, Comparison of our apo HKU1-A spike (S) structure (in grey) with the previously published structure of full-length HKU1-B spike (dark pink)27. b, Comparison of our HKU1-A S1B domain structure with the previously published HKU1-A S1B domain crystal structure (purple)24. c, Molecular dynamics (MD)-derived glycan coverage map of the HKU1 spike ectodomain (250 ns, 310 K). Full N-glycans (as shown for chain A, see Supplementary Fig. 16a) were attached based on previously published data31 where available. The spike protomers are coloured grey, blue and yellow and the N-linked glycans and bound disialoside (Sia) are coloured green and pink, respectively. To highlight the dynamics of the N-glycans, 250 snapshots extracted at time intervals of 1 ns are shown overlayed. d, Surface representation of the apo HKU1-A sialic acid binding site. Residues critical for sialic acid binding are coloured ruby and selected e1 loop residues are coloured blue. The location of the p1 and p2 pockets are indicated. e, Surface representation of the HKU1-B sialic acid binding site (PDB ID: 5I08)27, same colouring as panel d.
