Table 1.
H3
human
|
H5 avian
|
H9 swine
|
||||
---|---|---|---|---|---|---|
2,3 | 2,6 | 2,3 | 2,6 | 2,3 | 2,6 | |
98Y | Y-Sia1 | Y-Sia1 | Y-Sia1 | Y-Sia1 | Y-Sia1 | Y-Sia1 |
131 | S-Glc5 | |||||
133 | S-Glc5 | |||||
133a | S-Sia1 | S-Sia1 | ||||
134 | G-Sia1 | G-Sia1 | G-Sia1 | G-Sia1 | G-Sia1, G-Glc5 | |
135mc | G-Sia1 | G-Sia1 | V-Sia1 | V-Sia1 | T-Sia1 | T-Sia1, T-Glc5 |
136S | S-Sia1 | S-Sia1 | S-Sia1 | S-Sia1 | S-Sia1 | S-Sia1 |
137mc | N-Sia1 | N-Sia1 | S-Sia1 | S-Sia1 | K-Sia1, K-Gal2 | K-Sia1 |
153W | W-Sia1 | W-Sia1 | W-Sia1 | W-Sia1 | W-Sia1 | W-Sia1 |
155 | T-Sia1 | T-Sia1 | I-Sia1 | I-Sia1 | T-Sia1 | T-Sia1, T-Gal4 |
156 | K-Glc5 | Q-Gal4 | ||||
158 | G-Glc5 | |||||
165 | CHO-NAG3 | |||||
183 | H-Sia1 | H-Sia1 | H-Sia1 | H-Sia1 | ||
186 | N-Sia1 | P-Sia1 | P-Sia1 | |||
189 | Q-Gal4 | |||||
190 | E-Sia1 | E-Sia1 | E-Sia1, E-Gal2 | E-Sia1 | V-Sia1 | V-Sia1, V-NAG3 |
193 | S-Glc5 | N-NAG3, N-Gal4 | ||||
194L | L-Sia1 | L-Sia1 | L-Sia1 | L-Sia1 | L-Sia1 | L-Sia1, L-Gal4 |
222 | W-Gal2, W-NAG3 | |||||
225 | G-Gal2 | G-Gal2 | ||||
226 | L-Sia1, L-Gal2 | L-Sia1, L-Gal2 | Q-Sia1, Q-Gal2 | Q-Sia1 | L-Sia1, L-Gal2 | L-Sia1, L-Gal2 |
228 | S-Sia1 | S-Sia1 | H2O-Sia1 | H2O-Sia1 | H2O-Sia1 | H2O-Sia1 |
Receptor | ||||||
Sia1 | NAG3 | NAG3, Gal4, Glc5 | ||||
Gal2 | NAG3 |
Conserved interactions are underlined. Contacts with hydrogen bonds are in bold. The first column is the sequence according to H3 (X31) numbering. The first elements in each entry represent the amino acid at the corresponding position. Intramolecular interactions within the receptor are listed at the bottom of the table. At position 165 in H3/LSTa, the interaction is between NAG3 and the N linked CHO at Asn-165 across the trimeric interface. At position 228 in H5 and H9, a water molecule mediates the hydrogen bond from Sia1 and Gly-228.