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PDBsum entry 1rd8

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Viral protein PDB id
1rd8

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
328 a.a. *
175 a.a. *
Ligands
NAG-NAG-BMA ×2
NAG-NAG-BMA-MAN
NAG ×6
PO4
* Residue conservation analysis
PDB id:
1rd8
Name: Viral protein
Title: Crystal structure of the 1918 human h1 hemagglutinin precursor (ha0)
Structure: Hemagglutinin. Chain: a, c, e. Fragment: receptor binding domain, ha1 (residues 11-329). Engineered: yes. Hemagglutinin. Chain: b, d, f. Fragment: membrane fusion domain, ha2 (residues 1-175). Engineered: yes
Source: Influenza a virus. Organism_taxid: 11320. Gene: hemagglutinin. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Expression_system_cell_line: sf9.
Biol. unit: Hexamer (from PQS)
Resolution:
3.00Å     R-factor:   0.271     R-free:   0.295
Authors: J.Stevens,A.L.Corper,C.F.Basler,J.K.Taubenberger,P.Palese,I.A.Wilson
Key ref:
J.Stevens et al. (2004). Structure of the uncleaved human H1 hemagglutinin from the extinct 1918 influenza virus. Science, 303, 1866-1870. PubMed id: 14764887 DOI: 10.1126/science.1093373
Date:
05-Nov-03     Release date:   23-Mar-04    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9WFX3  (HEMA_I18A0) -  Hemagglutinin from Influenza A virus (strain A/Brevig Mission/1/1918 H1N1)
Seq:
Struc:
 
Seq:
Struc:
566 a.a.
328 a.a.*
Protein chains
Pfam   ArchSchema ?
Q9WFX3  (HEMA_I18A0) -  Hemagglutinin from Influenza A virus (strain A/Brevig Mission/1/1918 H1N1)
Seq:
Struc:
 
Seq:
Struc:
566 a.a.
175 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 

 
DOI no: 10.1126/science.1093373 Science 303:1866-1870 (2004)
PubMed id: 14764887  
 
 
Structure of the uncleaved human H1 hemagglutinin from the extinct 1918 influenza virus.
J.Stevens, A.L.Corper, C.F.Basler, J.K.Taubenberger, P.Palese, I.A.Wilson.
 
  ABSTRACT  
 
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.
 
  Selected figure(s)  
 
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).
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.
 
  The above figures are reprinted by permission from the AAAs: Science (2004, 303, 1866-1870) copyright 2004.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
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Structures of receptor complexes of a North American H7N2 influenza hemagglutinin with a loop deletion in the receptor binding site.
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PDB codes: 3m5g 3m5h 3m5i 3m5j
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Structure and Receptor binding properties of a pandemic H1N1 virus hemagglutinin.
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PDB code: 3m6s
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19837850 K.L.Hartshorn, M.R.White, T.Tecle, G.Sorensen, U.Holmskov, and E.C.Crouch (2010).
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20610681 M.S.Song, J.H.Lee, P.N.Pascua, Y.H.Baek, H.I.Kwon, K.J.Park, H.W.Choi, Y.K.Shin, J.Y.Song, C.J.Kim, and Y.K.Choi (2010).
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20660137 P.J.Carney, A.S.Lipatov, A.S.Monto, R.O.Donis, and J.Stevens (2010).
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  Science, 328, 357-360.
PDB codes: 3lzf 3lzg
20007271 R.Xu, R.McBride, J.C.Paulson, C.F.Basler, and I.A.Wilson (2010).
Structure, receptor binding, and antigenicity of influenza virus hemagglutinins from the 1957 H2N2 pandemic.
  J Virol, 84, 1715-1721.
PDB codes: 3ku3 3ku5 3ku6
20300625 V.A.Potdar, M.S.Chadha, S.M.Jadhav, J.Mullick, S.S.Cherian, and A.C.Mishra (2010).
Genetic characterization of the influenza A pandemic (H1N1) 2009 virus isolates from India.
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20602265 Y.Sun, Y.Shi, W.Zhang, Q.Li, D.Liu, C.Vavricka, J.Yan, and G.F.Gao (2010).
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Characterization of the influenza A H5N1 viruses of the 2008-09 outbreaks in India reveals a third introduction and possible endemicity.
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Recent strategies to identify broadly neutralizing antibodies against influenza A virus.
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19234466 J.Sui, W.C.Hwang, S.Perez, G.Wei, D.Aird, L.M.Chen, E.Santelli, B.Stec, G.Cadwell, M.Ali, H.Wan, A.Murakami, A.Yammanuru, T.Han, N.J.Cox, L.A.Bankston, R.O.Donis, R.C.Liddington, and W.A.Marasco (2009).
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PDB code: 3fku
19193808 M.L.Reed, H.L.Yen, R.M.DuBois, O.A.Bridges, R.Salomon, R.G.Webster, and C.J.Russell (2009).
Amino acid residues in the fusion peptide pocket regulate the pH of activation of the H5N1 influenza virus hemagglutinin protein.
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SeqMonitor: influenza analysis pipeline and visualization.
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19241254 O.Martinez, T.Tsibane, and C.F.Basler (2009).
Neutralizing anti-influenza virus monoclonal antibodies: therapeutics and tools for discovery.
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19399777 P.Das, J.Li, A.K.Royyuru, and R.Zhou (2009).
Free energy simulations reveal a double mutant avian H5N1 virus hemagglutinin with altered receptor binding specificity.
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19637916 P.M.Kasson, D.L.Ensign, and V.S.Pande (2009).
Combining molecular dynamics with bayesian analysis to predict and evaluate ligand-binding mutations in influenza hemagglutinin.
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18618705 Q.Huang, T.Korte, P.S.Rachakonda, E.W.Knapp, and A.Herrmann (2009).
Energetics of the loop-to-helix transition leading to the coiled-coil structure of influenza virus hemagglutinin HA2 subunits.
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The Polyomaviridae: Contributions of virus structure to our understanding of virus receptors and infectious entry.
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18176555 A.Chandrasekaran, A.Srinivasan, R.Raman, K.Viswanathan, S.Raguram, T.M.Tumpey, V.Sasisekharan, and R.Sasisekharan (2008).
Glycan topology determines human adaptation of avian H5N1 virus hemagglutinin.
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18287068 A.Srinivasan, K.Viswanathan, R.Raman, A.Chandrasekaran, S.Raguram, T.M.Tumpey, V.Sasisekharan, and R.Sasisekharan (2008).
Quantitative biochemical rationale for differences in transmissibility of 1918 pandemic influenza A viruses.
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18417563 C.J.Wei, L.Xu, W.P.Kong, W.Shi, K.Canis, J.Stevens, Z.Y.Yang, A.Dell, S.M.Haslam, I.A.Wilson, and G.J.Nabel (2008).
Comparative efficacy of neutralizing antibodies elicited by recombinant hemagglutinin proteins from avian H5N1 influenza virus.
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18568847 J.M.White, S.E.Delos, M.Brecher, and K.Schornberg (2008).
Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme.
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18672252 J.Stevens, O.Blixt, L.M.Chen, R.O.Donis, J.C.Paulson, and I.A.Wilson (2008).
Recent avian H5N1 viruses exhibit increased propensity for acquiring human receptor specificity.
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18621993 K.I.Hidari, T.Murata, K.Yoshida, Y.Takahashi, Y.H.Minamijima, Y.Miwa, S.Adachi, M.Ogata, T.Usui, Y.Suzuki, and T.Suzuki (2008).
Chemoenzymatic synthesis, characterization, and application of glycopolymers carrying lactosamine repeats as entry inhibitors against influenza virus infection.
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18811961 K.L.Hartshorn, R.Webby, M.R.White, T.Tecle, C.Pan, S.Boucher, R.J.Moreland, E.C.Crouch, and R.K.Scheule (2008).
Role of viral hemagglutinin glycosylation in anti-influenza activities of recombinant surfactant protein D.
  Respir Res, 9, 65.  
19756245 M.R.White, M.Doss, P.Boland, T.Tecle, and K.L.Hartshorn (2008).
Innate immunity to influenza virus: implications for future therapy.
  Expert Rev Clin Immunol, 4, 497-514.  
18184701 Q.Wang, F.Cheng, M.Lu, X.Tian, and J.Ma (2008).
Crystal structure of unliganded influenza B virus hemagglutinin.
  J Virol, 82, 3011-3020.
PDB code: 3bt6
18936253 R.Fritz, K.Stiasny, and F.X.Heinz (2008).
Identification of specific histidines as pH sensors in flavivirus membrane fusion.
  J Cell Biol, 183, 353-361.  
  19565017 T.Sawada, T.Hashimoto, H.Tokiwa, T.Suzuki, H.Nakano, H.Ishida, M.Kiso, and Y.Suzuki (2008).
Ab initio base fragment molecular orbital studies of influenza viral hemagglutinin HA1 full-domains in complex with sialoside receptors.
  J Mol Genet Med, 3, 133-142.  
18715929 X.Xu, X.Zhu, R.A.Dwek, J.Stevens, and I.A.Wilson (2008).
Structural characterization of the 1918 influenza virus H1N1 neuraminidase.
  J Virol, 82, 10493-10501.
PDB codes: 3b7e 3beq
18716625 X.Yu, T.Tsibane, P.A.McGraw, F.S.House, C.J.Keefer, M.D.Hicar, T.M.Tumpey, C.Pappas, L.A.Perrone, O.Martinez, J.Stevens, I.A.Wilson, P.V.Aguilar, E.L.Altschuler, C.F.Basler, and J.E.Crowe (2008).
Neutralizing antibodies derived from the B cells of 1918 influenza pandemic survivors.
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17443183 C.C.Wang, J.C.Lee, S.Y.Luo, S.S.Kulkarni, Y.W.Huang, C.C.Lee, K.L.Chang, and S.C.Hung (2007).
Regioselective one-pot protection of carbohydrates.
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17692139 G.A.Landolt, and C.W.Olsen (2007).
Up to new tricks - a review of cross-species transmission of influenza A viruses.
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The threat of avian influenza a (H5N1): part II: Clues to pathogenicity and pathology.
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The threat of avian influenza A (H5N1). Part I: Epidemiologic concerns and virulence determinants.
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Influence of calcium on lipid mixing mediated by influenza hemagglutinin.
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17636051 O.Loudig, E.Milova, M.Brandwein-Gensler, A.Massimi, T.J.Belbin, G.Childs, R.H.Singer, T.Rohan, and M.B.Prystowsky (2007).
Molecular restoration of archived transcriptional profiles by complementary-template reverse-transcription (CT-RT).
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17942670 Q.Wang, X.Tian, X.Chen, and J.Ma (2007).
Structural basis for receptor specificity of influenza B virus hemagglutinin.
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PDB codes: 2rft 2rfu
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Conformational change of influenza virus hemagglutinin is sensitive to ionic concentration.
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PDB code: 2b9b
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Pandemic avian influenza.
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Sialobiology of influenza: molecular mechanism of host range variation of influenza viruses.
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Cell surface biology mediated by low affinity multivalent protein-glycan interactions.
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Enhanced virulence of influenza A viruses with the haemagglutinin of the 1918 pandemic virus.
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The challenge of emerging and re-emerging infectious diseases.
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Confronting SARS: a view from Hong Kong.
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The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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