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PDBsum entry 1rd8
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Viral protein
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PDB id
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1rd8
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structure of the uncleaved human h1 hemagglutinin from the extinct 1918 influenza virus.
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Authors
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J.Stevens,
A.L.Corper,
C.F.Basler,
J.K.Taubenberger,
P.Palese,
I.A.Wilson.
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Ref.
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Science, 2004,
303,
1866-1870.
[DOI no: ]
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PubMed id
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Abstract
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The 1918 "Spanish" influenza pandemic represents the largest recorded
outbreak of any infectious disease. The crystal structure of the uncleaved
precursor of the major surface antigen of the extinct 1918 virus was determined
at 3.0 angstrom resolution after reassembly of the hemagglutinin gene from viral
RNA fragments preserved in 1918 formalin-fixed lung tissues. A narrow avian-like
receptor-binding site, two previously unobserved histidine patches, and a less
exposed surface loop at the cleavage site that activates viral membrane fusion
reveal structural features primarily found in avian viruses, which may have
contributed to the extraordinarily high infectivity and mortality rates observed
during 1918.
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Figure 2.
Fig. 2. Structural comparison of the 18HA0 cleavage site with
other HAs. HA2 domains for human H3 HA0 (PDB ID code: 1ha0 [PDB]
) and cleaved avian H5 HA1/HA2 (PDB ID code: 1jsm [PDB]
) (50) were aligned with 18HA0. The cleavage sites are colored
(A) green for human H3 HA0, (B) red for 18HA0 and (C) orange for
H5 HA1/HA2. RA329Q, ArgA329  GlnA329. (D)
Overlay of cleavage loops of H3 HA0, H1 HA0, and avian H5
HA1/HA2. The two views differ by a rotation of 90° about the
threefold vertical axis. (E) Surface views showing the trimer
interface and the position of the cleavage loop. (F) Removal of
the cleavage loop reveals the electronegative cavity that it
masks. Arg329 is colored blue and N-acetyl-glucosamines,
indicating the nearby glycosylation sites, are colored gold. (A)
to (D) were generated as in Fig. 1, and (E) and (F) were
generated with MSMS (46) through the program VMD (47).
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Figure 3.
Fig. 3. Structural comparisons of the environment around HA2
Trp21 in 18HA0 and H5 HA1/HA2. The avian H5 structure (PDB ID
code: 1jsm [PDB]
) was aligned with the 18HA0 model for comparison, as in Fig. 2.
In the avian structure (A), HisA18 and HisA38 are  3.7
Å apart, whereas in 18HA0 (B), the same residues are 13.5
Å apart. The TrpB21 "flip" in 18HA0 is stabilized by close
proximity to the side chains of TrpB14 and Ala^B36. This figure
was generated in the same way as Fig. 1A.
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The above figures are
reprinted
by permission from the AAAs:
Science
(2004,
303,
1866-1870)
copyright 2004.
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