| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T548 |
0-68 |
Sentence |
denotes |
Figure 6 Structural comparison of αCoV and βCoV spike (S) proteins. |
| T549 |
69-192 |
Sentence |
denotes |
Top and side views of homotrimeric S proteins, which are colored in salmon, marine and pale green, of αCoV (HCoV-NL63, pdb: |
| T550 |
193-233 |
Sentence |
denotes |
5szs [204]) (a) and βCoV (MERS-CoV, pdb: |
| T551 |
234-265 |
Sentence |
denotes |
6q06 [148] and 5x59 [205]) (b). |
| T552 |
266-522 |
Sentence |
denotes |
Notably, a difference in folding of the S1 subunit (white arrow) of each monomer of αCoV and βCoV S proteins results in a difference in positions of the S1-CTD subdomain, next to the S1-NTD subdomain in αCoV but substantially separated from S1-NTD in βCoV. |
| T553 |
523-682 |
Sentence |
denotes |
Consequently, the αCoV S trimer has a simple intra-subdomain packing, whereas βCoV has an intricate cross-subdomain packing as shown in the top and side views. |
| T554 |
683-742 |
Sentence |
denotes |
S1-NTD is located on the external surface of the S1 trimer. |
| T555 |
743-887 |
Sentence |
denotes |
S1-NTD, which functions as a receptor binding site, typically recognizes a host sugar receptor, except for MHV S1-NTD, which recognizes CEACAM1. |
| T556 |
888-979 |
Sentence |
denotes |
In contrast, S1-CTD is located on the internal surface of the S1 trimer in the lying state. |
| T557 |
980-1090 |
Sentence |
denotes |
S1-CTD can undergo dynamic conformational changes to the standing state for efficient binding to its receptor. |
| T558 |
1091-1161 |
Sentence |
denotes |
After binding, S1-CTD will be stabilized in the standing conformation. |
| T559 |
1162-1272 |
Sentence |
denotes |
So far, S1-CTD, which functions as a receptor binding site, has been found to bind to a host protein receptor. |
