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.
