Id |
Subject |
Object |
Predicate |
Lexical cue |
T106 |
0-487 |
Sentence |
denotes |
Structural comparison of avian-type and human-type receptors interacting with the receptor binding sites of avian H3/1963, pandemic (pdm) H3/1968 and human H3/2007 (Figure 3b) revealed that trisaccharide Neu5Acα2,3Galβ1,3GlcNAc of lactoseries tetrasaccharide a (LSTa) interacts with the avian H3/1963 binding site in a cone-like topology (1mqm [149]), whereas 6′SLNLN interacts with pandemic H3/1968 (6tzb [150]) and human H3/2007 binding sites in an umbrella-like topology (6aov [151]). |
T107 |
488-573 |
Sentence |
denotes |
Residues 226 and 228 are important in determining sialyl linkage binding specificity. |
T108 |
574-893 |
Sentence |
denotes |
As shown in Figure 3b, Q226 in the avian H3/1963 binding site directly forms hydrogen bonds with Sia-1 and Gal-2 of LSTa, whereas S228 in the pdm H3/1968 binding site directly forms a hydrogen bond with Sia-1 of 6′SLNLN and S228 in the human H3/2007 binding site directly forms two hydrogen bonds with Sia-1 of 6′SLNLN. |
T109 |
894-1072 |
Sentence |
denotes |
Although no direct interaction of residue 226 in pdm and human H3 HAs was found, a previous study suggested that L226Q mutation in the HA decreases α2,6Neu5Ac binding preference. |
T110 |
1073-1171 |
Sentence |
denotes |
Both G228 and S228 can be found in H3 avian HAs, whereas only S228 is found in human H3 HAs [149]. |
T111 |
1172-1312 |
Sentence |
denotes |
L226 is not conserved during circulation in humans; L226V and V226I substitutions were observed before 2001 and in 2004, respectively [160]. |