Author: Jinfang Yu; Shuyuan Qiao; Runyu Guo; Xinquan Wang
Title: Cryo-EM structures of HKU2 and SADS-CoV spike glycoproteins and insights into coronavirus evolution Document date: 2020_2_24
ID: 25va2cvt_28
Snippet: Conserved S2 subunit and a distinct CR 297 Sequence analysis suggested that the S1/S2 protease cleavage site at the boundary 298 between the S1 and S2 subunits is R544-M545 in HKU2 spike and R546-M547 in 299 SADS-CoV spike 5,8,47 . Compared to the S1 subunit, the topology and structure of S2 The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.02.23.961912 doi: bioRxiv preprint (residues 748-8.....
Document: Conserved S2 subunit and a distinct CR 297 Sequence analysis suggested that the S1/S2 protease cleavage site at the boundary 298 between the S1 and S2 subunits is R544-M545 in HKU2 spike and R546-M547 in 299 SADS-CoV spike 5,8,47 . Compared to the S1 subunit, the topology and structure of S2 The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.02.23.961912 doi: bioRxiv preprint (residues 748-836), a central helix (CH) (residues 837-887), a twisted β-hairpin (BH) 304 (residues 888-929) and a β-sandwich like SD3 (residues 930-995) (Fig. 1b and Fig. 6a) . 305 Like in other coronavirus spikes in the prefusion state, the model of HR2 after SD3 was 306 not built in the structure due to poor density. Five disulfide bonds in S2 are detected.
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