 |
PDBsum entry 1rvx
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Viral protein
|
PDB id
|
|
|
|
1rvx
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
(+ 0 more)
323 a.a.
|
|
|
|
|
|
|
|
|
|
|
(+ 0 more)
160 a.a.
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
The structure and receptor binding properties of the 1918 influenza hemagglutinin.
|
|
|
Authors
|
|
S.J.Gamblin,
L.F.Haire,
R.J.Russell,
D.J.Stevens,
B.Xiao,
Y.Ha,
N.Vasisht,
D.A.Steinhauer,
R.S.Daniels,
A.Elliot,
D.C.Wiley,
J.J.Skehel.
|
|
|
Ref.
|
|
Science, 2004,
303,
1838-1842.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
The 1918 influenza pandemic resulted in about 20 million deaths. This enormous
impact, coupled with renewed interest in emerging infections, makes
characterization of the virus involved a priority. Receptor binding, the initial
event in virus infection, is a major determinant of virus transmissibility that,
for influenza viruses, is mediated by the hemagglutinin (HA) membrane
glycoprotein. We have determined the crystal structures of the HA from the 1918
virus and two closely related HAs in complex with receptor analogs. They explain
how the 1918 HA, while retaining receptor binding site amino acids
characteristic of an avian precursor HA, is able to bind human receptors and
how, as a consequence, the virus was able to spread in the human population.
|
|
|
|
|
|
|
|
Figure 1.
Fig. 1. Sequence alignment of 1918-human, 1930-swine, and
1934-human HAs. The subdomain structure of HA in the two
polypeptides, HA1 and HA2, that form each monomer is indicated
by the colored bars above the sequences. Carbohydrate attachment
sites are shaded gray. Residue numbering is on the basis of H3
HA sequence (1). Nonconserved residues are in red.
|
|
Figure 5.
Fig. 5. Superposition of the binding site of 1934-human HA in
its uncomplexed state and complexed with avian receptor analog.
The HA is shown in green in both cases, and the avian receptor
is colored as in Fig. 3. Two water molecules, shown as green
spheres, link Glu190 to Gln226 in the avian receptor complex.
This hydrogen-bonded network is not formed in the uncomplexed
structure or in the human receptor complex not shown.
|
|
|
|
|
|
The above figures are
reprinted
by permission from the AAAs:
Science
(2004,
303,
1838-1842)
copyright 2004.
|
|
|
|
|
|
|
