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PDBsum entry 4eda
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Viral protein
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PDB id
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4eda
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Contents |
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321 a.a.
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148 a.a.
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115 a.a.
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PDB id:
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| Name: |
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Viral protein
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Title:
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Structures of monomeric hemagglutinin and its complex with an fab fragment of a neutralizing antibody that binds to h1 subtype influenza viruses: molecular basis of infectivity of 2009 pandemic h1n1 influenza a viruses
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Structure:
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Hemagglutinin. Chain: a, c. Fragment: ha1 subunit, unp residues 18-344. Engineered: yes. Hemagglutinin. Chain: b, d. Fragment: ha2 subunit, unp residues 345-520. Engineered: yes
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Source:
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Influenza a virus. Organism_taxid: 644289. Strain: a/korea/01/2009 h1n1. Gene: ha. Expressed in: trichoplusia ni. Expression_system_taxid: 7111. Expression_system_cell_line: hi5.
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Resolution:
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2.70Å
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R-factor:
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0.240
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R-free:
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0.289
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Authors:
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K.H.Kim,K.J.Cho,J.H.Lee,Y.H.Park,T.G.Khan,J.Y.Lee,S.H.Kang,I.Alam
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Key ref:
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K.J.Cho
et al.
(2013).
Insight into structural diversity of influenza virus haemagglutinin.
J Gen Virol,
94,
1712-1722.
PubMed id:
DOI:
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Date:
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27-Mar-12
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Release date:
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22-May-13
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PROCHECK
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Headers
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References
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C5MQE6
(C5MQE6_9INFA) -
Hemagglutinin from Influenza A virus
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Seq:
Struc:
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566 a.a.
321 a.a.
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DOI no:
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J Gen Virol
94:1712-1722
(2013)
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PubMed id:
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Insight into structural diversity of influenza virus haemagglutinin.
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K.J.Cho,
J.H.Lee,
K.W.Hong,
S.H.Kim,
Y.Park,
J.Y.Lee,
S.Kang,
S.Kim,
J.H.Yang,
E.K.Kim,
J.H.Seok,
S.Unzai,
S.Y.Park,
X.Saelens,
C.J.Kim,
J.Y.Lee,
C.Kang,
H.B.Oh,
M.S.Chung,
K.H.Kim.
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ABSTRACT
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Influenza virus infects host cells through membrane fusion, a process mediated
by the low pH-induced conformational change of the viral surface glycoprotein
haemagglutinin (HA). We determined the structures and biochemical properties of
the HA proteins from A/Korea/01/2009 (KR01), a 2009 pandemic strain, and
A/Thailand/CU44/2006 (CU44), a seasonal strain. The crystal structure of KR01 HA
revealed a V-shaped head-to-head arrangement, which is not seen in other HA
proteins including CU44 HA. We isolated a broadly neutralizing H1-specific
monoclonal antibody GC0757. The KR01 HA-Fab0757 complex structure also exhibited
a head-to-head arrangement of HA. Both native and Fab complex structures reveal
a different spatial orientation of HA1 relative to HA2, indicating that HA is
flexible and dynamic at neutral pH. Further, the KR01 HA exhibited significantly
lower protein stability and increased susceptibility to proteolytic cleavage
compared with other HAs. Our structures provide important insights into the
conformational flexibility of HA.
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Links
