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PDBsum entry 1e8v

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
1e8v
Jmol
Contents
Protein chains
447 a.a. *
Ligands
DAN ×2
NAG ×3
NAG-NAG
Metals
_CA ×2
Waters ×239
* Residue conservation analysis
PDB id:
1e8v
Name: Hydrolase
Title: Structure of the multifunctional paramyxovirus hemagglutinin-neuraminidase
Structure: Hemagglutinin-neuraminidase. Chain: a, b. Fragment: head domain, residues 124-577. Synonym: hn. Ec: 3.2.1.18
Source: Newcastle disease virus. Organism_taxid: 11176. Strain: kansas
Biol. unit: Homo-Dimer (from PDB file)
Resolution:
2.00Å     R-factor:   0.232     R-free:   0.267
Authors: S.Crennell,T.Takimoto,A.Portner,G.Taylor
Key ref:
S.Crennell et al. (2000). Crystal structure of the multifunctional paramyxovirus hemagglutinin-neuraminidase. Nat Struct Biol, 7, 1068-1074. PubMed id: 11062565 DOI: 10.1038/81002
Date:
01-Oct-00     Release date:   03-Apr-01    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9Q2W5  (HN_NDVK) -  Hemagglutinin-neuraminidase
Seq:
Struc:
 
Seq:
Struc:
577 a.a.
447 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.18  - Exo-alpha-sialidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)-glycosidic linkages of terminal sialic residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     viral envelope   1 term 
  Biological process     viral infectious cycle   1 term 
  Biochemical function     host cell surface receptor binding     2 terms  

 

 
DOI no: 10.1038/81002 Nat Struct Biol 7:1068-1074 (2000)
PubMed id: 11062565  
 
 
Crystal structure of the multifunctional paramyxovirus hemagglutinin-neuraminidase.
S.Crennell, T.Takimoto, A.Portner, G.Taylor.
 
  ABSTRACT  
 
Paramyxoviruses are the main cause of respiratory disease in children. One of two viral surface glycoproteins, the hemagglutinin-neuraminidase (HN), has several functions in addition to being the major surface antigen that induces neutralizing antibodies. Here we present the crystal structures of Newcastle disease virus HN alone and in complex with either an inhibitor or with the beta-anomer of sialic acid. The inhibitor complex reveals a typical neuraminidase active site within a beta-propeller fold. Comparison of the structures of the two complexes reveal differences in the active site, suggesting that the catalytic site is activated by a conformational switch. This site may provide both sialic acid binding and hydrolysis functions since there is no evidence for a second sialic acid binding site in HN. Evidence for a single site with dual functions is examined and supported by mutagenesis studies. The structure provides the basis for the structure-based design of inhibitors for a range of paramyxovirus-induced diseases.
 
  Selected figure(s)  
 
Figure 1.
Figure 1. Schematic representations of the crystal structure of HN. The chains are colored from blue at the N-terminus through to red at the C-terminus. The N-linked carbohydrate residues are shown in ball and stick representation, and the divalent metal ions are drawn as gray spheres. a, The HN dimer observed in the orthorhombic crystal form, viewed down the NCS two-fold axis showing the location of the -anomer of sialic acid drawn as a space filling molecule. b, The dimer of the HN -Neu5Ac2en complex observed in the hexagonal crystal form, viewed down the NCS two-fold axis. c, The image in (b) rotated by 45 around a horizontal axis and colored according to B-factor conveniently reveals orthogonal views of the HN monomer. Coloring is from dark blue (B = 10 2) to deep red (B = 60 2).
Figure 3.
Figure 3. The active site. a, The inhibitor Neu5Ac2en bound in the active site of the hexagonal crystal form. b, The same active site as observed in the ligand-free pH 4.6 orthorhombic crystal structure. c, The -anomer of sialic acid bound in the active site of the pH 4.6 orthorhombic crystal form, showing hydrogen bonding interactions (dotted lines). Water molecules are labeled W.
 
  The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Biol (2000, 7, 1068-1074) copyright 2000.  
  Figures were selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21123551 C.Estevez, D.J.King, M.Luo, and Q.Yu (2011).
A single amino acid substitution in the haemagglutinin-neuraminidase protein of Newcastle disease virus results in increased fusion promotion and decreased neuraminidase activities without changes in virus pathotype.
  J Gen Virol, 92, 544-551.  
21217701 C.K.Navaratnarajah, N.Oezguen, L.Rupp, L.Kay, V.H.Leonard, W.Braun, and R.Cattaneo (2011).
The heads of the measles virus attachment protein move to transmit the fusion-triggering signal.
  Nat Struct Mol Biol, 18, 128-134.  
21152939 S.H.Shi, Y.Huang, S.J.Cui, L.F.Cheng, G.H.Fu, X.Li, Z.Chen, C.X.Peng, F.Lin, J.S.Lin, and J.L.Su (2011).
Genomic sequence of an avian paramyxovirus type 1 strain isolated from Muscovy duck (Cairina moschata) in China.
  Arch Virol, 156, 405-412.  
21058397 S.Indu, V.Kochat, S.Thakurela, C.Ramakrishnan, and R.Varadarajan (2011).
Conformational analysis and design of cross-strand disulfides in antiparallel β-sheets.
  Proteins, 79, 244-260.  
20024589 C.A Baumann, and W.J Neubert (2010).
Neuraminidase-deficient Sendai virus HN mutants provide protection from homologous superinfection.
  Arch Virol, 155, 217-227.  
20010840 C.Santiago, M.L.Celma, T.Stehle, and J.M.Casasnovas (2010).
Structure of the measles virus hemagglutinin bound to the CD46 receptor.
  Nat Struct Mol Biol, 17, 124-129.
PDB code: 3inb
20382985 G.L.Taylor (2010).
Introduction to phasing.
  Acta Crystallogr D Biol Crystallogr, 66, 325-338.  
20631152 L.Zipperle, J.P.Langedijk, C.Orvell, M.Vandevelde, A.Zurbriggen, and P.Plattet (2010).
Identification of key residues in virulent canine distemper virus hemagglutinin that control CD150/SLAM-binding activity.
  J Virol, 84, 9618-9624.  
20009427 R.Tsunekun, H.Ito, H.Kida, K.Otsuki, and T.Ito (2010).
Increase in the Neuraminidase Activity of a Nonpathogenic Newcastle Disease Virus Isolate during Passaging in Chickens.
  J Vet Med Sci, 72, 453-457.  
20375167 T.A.Bowden, M.Crispin, D.J.Harvey, E.Y.Jones, and D.I.Stuart (2010).
Dimeric architecture of the Hendra virus attachment glycoprotein: evidence for a conserved mode of assembly.
  J Virol, 84, 6208-6217.
PDB code: 2x9m
20053750 V.P.Mishin, M.Watanabe, G.Taylor, J.Devincenzo, M.Bose, A.Portner, and I.V.Alymova (2010).
N-linked glycan at residue 523 of human parainfluenza virus type 3 hemagglutinin-neuraminidase masks a second receptor-binding site.
  J Virol, 84, 3094-3100.  
20661635 Z.Ding, Y.L.Cong, S.Chang, G.M.Wang, Z.Wang, Q.P.Zhang, H.Wu, and Y.Z.Sun (2010).
Genetic analysis of avian paramyxovirus-1 (Newcastle disease virus) isolates obtained from swine populations in China related to commonly utilized commercial vaccine strains.
  Virus Genes, 41, 369-376.  
19052089 A.Krishnan, S.K.Verma, P.Mani, R.Gupta, S.Kundu, and D.P.Sarkar (2009).
A histidine switch in hemagglutinin-neuraminidase triggers paramyxovirus-cell membrane fusion.
  J Virol, 83, 1727-1741.  
19337823 D.Qiao, B.H.Janke, and S.Elankumaran (2009).
Molecular characterization of glycoprotein genes and phylogenetic analysis of two swine paramyxoviruses isolated from United States.
  Virus Genes, 39, 53-65.  
19031463 D.Shah, S.Vidal, M.A.Link, S.A.Rubin, and K.E.Wright (2009).
Identification of genetic mutations associated with attenuation and changes in tropism of Urabe mumps virus.
  J Med Virol, 81, 130-138.  
19878307 E.C.Smith, A.Popa, A.Chang, C.Masante, and R.E.Dutch (2009).
Viral entry mechanisms: the increasing diversity of paramyxovirus entry.
  FEBS J, 276, 7217-7227.  
19019819 H.C.Aguilar, Z.A.Ataman, V.Aspericueta, A.Q.Fang, M.Stroud, O.A.Negrete, R.A.Kammerer, and B.Lee (2009).
A Novel Receptor-induced Activation Site in the Nipah Virus Attachment Glycoprotein (G) Involved in Triggering the Fusion Glycoprotein (F).
  J Biol Chem, 284, 1628-1635.  
  19918093 I.V.Alymova, M.Watanabe, K.L.Boyd, P.Chand, Y.S.Babu, and A.Portner (2009).
Efficacy of the novel parainfluenza virus haemagglutinin-neuraminidase inhibitor BCX 2798 in mice - further evaluation.
  Antivir Ther, 14, 891-898.  
19208223 J.Mast, and L.Demeestere (2009).
Electron tomography of negatively stained complex viruses: application in their diagnosis.
  Diagn Pathol, 4, 5.  
19515783 M.Jarahian, C.Watzl, P.Fournier, A.Arnold, D.Djandji, S.Zahedi, A.Cerwenka, A.Paschen, V.Schirrmacher, and F.Momburg (2009).
Activation of natural killer cells by newcastle disease virus hemagglutinin-neuraminidase.
  J Virol, 83, 8108-8121.  
19564364 M.Watanabe, V.P.Mishin, S.A.Brown, C.J.Russell, K.Boyd, Y.S.Babu, G.Taylor, X.Xiong, X.Yan, A.Portner, and I.V.Alymova (2009).
Effect of hemagglutinin-neuraminidase inhibitors BCX 2798 and BCX 2855 on growth and pathogenicity of Sendai/human parainfluenza type 3 chimera virus in mice.
  Antimicrob Agents Chemother, 53, 3942-3951.  
  20161127 R.M.Iorio, V.R.Melanson, and P.J.Mahon (2009).
Glycoprotein interactions in paramyxovirus fusion.
  Future Virol, 4, 335-351.  
19710150 S.A.Connolly, G.P.Leser, T.S.Jardetzky, and R.A.Lamb (2009).
Bimolecular complementation of paramyxovirus fusion and hemagglutinin-neuraminidase proteins enhances fusion: implications for the mechanism of fusion triggering.
  J Virol, 83, 10857-10868.  
19474107 S.K.Khattar, Y.Yan, A.Panda, P.L.Collins, and S.K.Samal (2009).
A Y526Q mutation in the Newcastle disease virus HN protein reduces its functional activities and attenuates virus replication and pathogenicity.
  J Virol, 83, 7779-7782.  
19656895 T.Paal, M.A.Brindley, C.St Clair, A.Prussia, D.Gaus, S.A.Krumm, J.P.Snyder, and R.K.Plemper (2009).
Probing the spatial organization of measles virus fusion complexes.
  J Virol, 83, 10480-10493.  
19342221 T.Stehle, and J.M.Casasnovas (2009).
Specificity switching in virus-receptor complexes.
  Curr Opin Struct Biol, 19, 181-188.  
19157478 U.Neu, T.Stehle, and W.J.Atwood (2009).
The Polyomaviridae: Contributions of virus structure to our understanding of virus receptors and infectious entry.
  Virology, 384, 389-399.  
18292085 C.K.Navaratnarajah, S.Vongpunsawad, N.Oezguen, T.Stehle, W.Braun, T.Hashiguchi, K.Maenaka, Y.Yanagi, and R.Cattaneo (2008).
Dynamic interaction of the measles virus hemagglutinin with its receptor signaling lymphocytic activation molecule (SLAM, CD150).
  J Biol Chem, 283, 11763-11771.  
18063573 E.Severi, A.Müller, J.R.Potts, A.Leech, D.Williamson, K.S.Wilson, and G.H.Thomas (2008).
Sialic acid mutarotation is catalyzed by the Escherichia coli beta-propeller protein YjhT.
  J Biol Chem, 283, 4841-4849.
PDB code: 2uvk
18579600 I.V.Alymova, G.Taylor, V.P.Mishin, M.Watanabe, K.G.Murti, K.Boyd, P.Chand, Y.S.Babu, and A.Portner (2008).
Loss of the N-linked glycan at residue 173 of human parainfluenza virus type 1 hemagglutinin-neuraminidase exposes a second receptor-binding site.
  J Virol, 82, 8400-8410.  
18426797 J.K.Lee, A.Prussia, T.Paal, L.K.White, J.P.Snyder, and R.K.Plemper (2008).
Functional interaction between paramyxovirus fusion and attachment proteins.
  J Biol Chem, 283, 16561-16572.  
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.
  Crit Rev Biochem Mol Biol, 43, 189-219.  
18799571 K.A.Bishop, A.C.Hickey, D.Khetawat, J.R.Patch, K.N.Bossart, Z.Zhu, L.F.Wang, D.S.Dimitrov, and C.C.Broder (2008).
Residues in the stalk domain of the hendra virus g glycoprotein modulate conformational changes associated with receptor binding.
  J Virol, 82, 11398-11409.  
18632560 K.Xu, K.R.Rajashankar, Y.P.Chan, J.P.Himanen, C.C.Broder, and D.B.Nikolov (2008).
Host cell recognition by the henipaviruses: crystal structures of the Nipah G attachment glycoprotein and its complex with ephrin-B3.
  Proc Natl Acad Sci U S A, 105, 9953-9958.
PDB codes: 3d11 3d12
18753211 P.J.Mahon, A.M.Mirza, T.A.Musich, and R.M.Iorio (2008).
Engineered intermonomeric disulfide bonds in the globular domain of Newcastle disease virus hemagglutinin-neuraminidase protein: implications for the mechanism of fusion promotion.
  J Virol, 82, 10386-10396.  
18346895 R.M.Iorio, and P.J.Mahon (2008).
Paramyxoviruses: different receptors - different mechanisms of fusion.
  Trends Microbiol, 16, 135-137.  
18218621 S.L.Newstead, J.A.Potter, J.C.Wilson, G.Xu, C.H.Chien, A.G.Watts, S.G.Withers, and G.L.Taylor (2008).
The structure of Clostridium perfringens NanI sialidase and its catalytic intermediates.
  J Biol Chem, 283, 9080-9088.
PDB codes: 2bf6 2vk5 2vk6 2vk7
18488039 T.A.Bowden, A.R.Aricescu, R.J.Gilbert, J.M.Grimes, E.Y.Jones, and D.I.Stuart (2008).
Structural basis of Nipah and Hendra virus attachment to their cell-surface receptor ephrin-B2.
  Nat Struct Mol Biol, 15, 567-572.
PDB codes: 2vsk 2vsm
18815311 T.A.Bowden, M.Crispin, D.J.Harvey, A.R.Aricescu, J.M.Grimes, E.Y.Jones, and D.I.Stuart (2008).
Crystal structure and carbohydrate analysis of Nipah virus attachment glycoprotein: a template for antiviral and vaccine design.
  J Virol, 82, 11628-11636.
PDB code: 2vwd
19122383 T.Hashiguchi, K.Maenaka, and Y.Yanagi (2008).
X-ray crystallographic analysis of measles virus hemagglutinin.
  Uirusu, 58, 1.  
18499307 X.Zhan, K.S.Slobod, S.Krishnamurthy, L.E.Luque, T.Takimoto, B.Jones, S.Surman, C.J.Russell, A.Portner, and J.L.Hurwitz (2008).
Sendai virus recombinant vaccine expressing hPIV-3 HN or F elicits protective immunity and combines with a second recombinant to prevent hPIV-1, hPIV-3 and RSV infections.
  Vaccine, 26, 3480-3488.  
18026116 L.A.Colf, Z.S.Juo, and K.C.Garcia (2007).
Structure of the measles virus hemagglutinin.
  Nat Struct Mol Biol, 14, 1227-1228.  
17470652 L.K.White, J.J.Yoon, J.K.Lee, A.Sun, Y.Du, H.Fu, J.P.Snyder, and R.K.Plemper (2007).
Nonnucleoside inhibitor of measles virus RNA-dependent RNA polymerase complex activity.
  Antimicrob Agents Chemother, 51, 2293-2303.  
17567695 L.M.Palermo, M.Porotto, O.Greengard, and A.Moscona (2007).
Fusion promotion by a paramyxovirus hemagglutinin-neuraminidase protein: pH modulation of receptor avidity of binding sites I and II.
  J Virol, 81, 9152-9161.  
17585869 M.A.Zhukovsky, I.Markovic, and A.L.Bailey (2007).
Influence of calcium on lipid mixing mediated by influenza hemagglutinin.
  Arch Biochem Biophys, 465, 101-108.  
17229690 M.Porotto, M.Fornabaio, G.E.Kellogg, and A.Moscona (2007).
A second receptor binding site on human parainfluenza virus type 3 hemagglutinin-neuraminidase contributes to activation of the fusion mechanism.
  J Virol, 81, 3216-3228.  
17318427 S.H.Cho, S.J.Kim, and H.J.Kwon (2007).
Genomic sequence of an antigenic variant Newcastle disease virus isolated in Korea.
  Virus Genes, 35, 293-302.  
18003910 T.Hashiguchi, M.Kajikawa, N.Maita, M.Takeda, K.Kuroki, K.Sasaki, D.Kohda, Y.Yanagi, and K.Maenaka (2007).
Crystal structure of measles virus hemagglutinin provides insight into effective vaccines.
  Proc Natl Acad Sci U S A, 104, 19535-19540.
PDB codes: 2zb5 2zb6
16702222 A.Müller, E.Severi, C.Mulligan, A.G.Watts, D.J.Kelly, K.S.Wilson, A.J.Wilkinson, and G.H.Thomas (2006).
Conservation of structure and mechanism in primary and secondary transporters exemplified by SiaP, a sialic acid binding virulence factor from Haemophilus influenzae.
  J Biol Chem, 281, 22212-22222.
PDB codes: 2cex 2cey
16357858 B.T.Eaton, C.C.Broder, D.Middleton, and L.F.Wang (2006).
Hendra and Nipah viruses: different and dangerous.
  Nat Rev Microbiol, 4, 23-35.  
16678421 C.J.Russell, and L.E.Luque (2006).
The structural basis of paramyxovirus invasion.
  Trends Microbiol, 14, 243-246.  
16575531 C.Ryan, V.Zaitsev, D.J.Tindal, J.C.Dyason, R.J.Thomson, I.Alymova, A.Portner, M.von Itzstein, and G.Taylor (2006).
Structural analysis of a designed inhibitor complexed with the hemagglutinin-neuraminidase of Newcastle disease virus.
  Glycoconj J, 23, 135-141.  
16575518 E.Villar, and I.M.Barroso (2006).
Role of sialic acid-containing molecules in paramyxovirus entry into the host cell: a minireview.
  Glycoconj J, 23, 5.  
16230015 H.Streicher, and H.Busse (2006).
Building a successful structural motif into sialylmimetics-cyclohexenephosphonate monoesters as pseudo-sialosides with promising inhibitory properties.
  Bioorg Med Chem, 14, 1047-1057.  
16501098 L.W.McGinnes, and T.G.Morrison (2006).
Inhibition of receptor binding stabilizes Newcastle disease virus HN and F protein-containing complexes.
  J Virol, 80, 2894-2903.  
16414997 M.Porotto, M.Fornabaio, O.Greengard, M.T.Murrell, G.E.Kellogg, and A.Moscona (2006).
Paramyxovirus receptor-binding molecules: engagement of one site on the hemagglutinin-neuraminidase protein modulates activity at the second site.
  J Virol, 80, 1204-1213.  
17093041 S.A.Connolly, G.P.Leser, H.S.Yin, T.S.Jardetzky, and R.A.Lamb (2006).
Refolding of a paramyxovirus F protein from prefusion to postfusion conformations observed by liposome binding and electron microscopy.
  Proc Natl Acad Sci U S A, 103, 17903-17908.  
16940513 T.Bousse, and T.Takimoto (2006).
Mutation at residue 523 creates a second receptor binding site on human parainfluenza virus type 1 hemagglutinin-neuraminidase protein.
  J Virol, 80, 9009-9016.  
16840334 V.Guillaume, H.Aslan, M.Ainouze, M.Guerbois, T.F.Wild, R.Buckland, and J.P.Langedijk (2006).
Evidence of a potential receptor-binding site on the Nipah virus G protein (NiV-G): identification of globular head residues with a role in fusion promotion and their localization on an NiV-G structural model.
  J Virol, 80, 7546-7554.  
16378965 V.R.Melanson, and R.M.Iorio (2006).
Addition of N-glycans in the stalk of the Newcastle disease virus HN protein blocks its interaction with the F protein and prevents fusion.
  J Virol, 80, 623-633.  
16007245 A.Moscona (2005).
Entry of parainfluenza virus into cells as a target for interrupting childhood respiratory disease.
  J Clin Invest, 115, 1688-1698.  
15605385 C.J.Jeffery (2005).
Mass spectrometry and the search for moonlighting proteins.
  Mass Spectrom Rev, 24, 772-782.  
15616320 I.V.Alymova, A.Portner, T.Takimoto, K.L.Boyd, Y.S.Babu, and J.A.McCullers (2005).
The novel parainfluenza virus hemagglutinin-neuraminidase inhibitor BCX 2798 prevents lethal synergism between a paramyxovirus and Streptococcus pneumoniae.
  Antimicrob Agents Chemother, 49, 398-405.  
15864320 J.N.Watson, T.L.Knoll, J.H.Chen, D.T.Chou, T.J.Borgford, and A.J.Bennet (2005).
Use of conformationally restricted pyridinium alpha-D-N-acetylneuraminides to probe specificity in bacterial and viral sialidases.
  Biochem Cell Biol, 83, 115-122.  
15890907 K.N.Bossart, G.Crameri, A.S.Dimitrov, B.A.Mungall, Y.R.Feng, J.R.Patch, A.Choudhary, L.F.Wang, B.T.Eaton, and C.C.Broder (2005).
Receptor binding, fusion inhibition, and induction of cross-reactive neutralizing antibodies by a soluble G glycoprotein of Hendra virus.
  J Virol, 79, 6690-6702.  
15608653 K.Stummeyer, A.Dickmanns, M.Mühlenhoff, R.Gerardy-Schahn, and R.Ficner (2005).
Crystal structure of the polysialic acid-degrading endosialidase of bacteriophage K1F.
  Nat Struct Mol Biol, 12, 90-96.
PDB codes: 1v0e 1v0f
15998730 M.I.Bonaparte, A.S.Dimitrov, K.N.Bossart, G.Crameri, B.A.Mungall, K.A.Bishop, V.Choudhry, D.S.Dimitrov, L.F.Wang, B.T.Eaton, and C.C.Broder (2005).
Ephrin-B2 ligand is a functional receptor for Hendra virus and Nipah virus.
  Proc Natl Acad Sci U S A, 102, 10652-10657.  
15681439 M.Porotto, M.Murrell, O.Greengard, L.Doctor, and A.Moscona (2005).
Influence of the human parainfluenza virus 3 attachment protein's neuraminidase activity on its capacity to activate the fusion protein.
  J Virol, 79, 2383-2392.  
16557006 M.Tsurudome (2005).
[Viral fusion mechanisms]
  Uirusu, 55, 207-219.  
15893670 P.Yuan, T.B.Thompson, B.A.Wurzburg, R.G.Paterson, R.A.Lamb, and T.S.Jardetzky (2005).
Structural studies of the parainfluenza virus 5 hemagglutinin-neuraminidase tetramer in complex with its receptor, sialyllactose.
  Structure, 13, 803-815.
PDB codes: 1z4v 1z4w 1z4x 1z4y 1z4z 1z50
15827201 V.von Messling, N.Oezguen, Q.Zheng, S.Vongpunsawad, W.Braun, and R.Cattaneo (2005).
Nearby clusters of hemagglutinin residues sustain SLAM-dependent canine distemper virus entry in peripheral blood mononuclear cells.
  J Virol, 79, 5857-5862.  
15073366 A.E.Smith, and A.Helenius (2004).
How viruses enter animal cells.
  Science, 304, 237-242.  
15564482 C.J.Russell, T.S.Jardetzky, and R.A.Lamb (2004).
Conserved glycine residues in the fusion peptide of the paramyxovirus fusion protein regulate activation of the native state.
  J Virol, 78, 13727-13742.  
14730352 C.P.Chiu, A.G.Watts, L.L.Lairson, M.Gilbert, D.Lim, W.W.Wakarchuk, S.G.Withers, and N.C.Strynadka (2004).
Structural analysis of the sialyltransferase CstII from Campylobacter jejuni in complex with a substrate analog.
  Nat Struct Mol Biol, 11, 163-170.
PDB codes: 1ro7 1ro8
15197264 D.L.Waning, C.J.Russell, T.S.Jardetzky, and R.A.Lamb (2004).
Activation of a paramyxovirus fusion protein is modulated by inside-out signaling from the cytoplasmic tail.
  Proc Natl Acad Sci U S A, 101, 9217-9222.  
15016875 E.Escribano-Romero, J.Rawling, B.García-Barreno, and J.A.Melero (2004).
The soluble form of human respiratory syncytial virus attachment protein differs from the membrane-bound form in its oligomeric state but is still capable of binding to cell surface proteoglycans.
  J Virol, 78, 3524-3532.  
15226294 I.Moustafa, H.Connaris, M.Taylor, V.Zaitsev, J.C.Wilson, M.J.Kiefel, M.von Itzstein, and G.Taylor (2004).
Sialic acid recognition by Vibrio cholerae neuraminidase.
  J Biol Chem, 279, 40819-40826.
PDB codes: 1w0o 1w0p
15105096 I.V.Alymova, G.Taylor, T.Takimoto, T.H.Lin, P.Chand, Y.S.Babu, C.Li, X.Xiong, and A.Portner (2004).
Efficacy of novel hemagglutinin-neuraminidase inhibitors BCX 2798 and BCX 2855 against human parainfluenza viruses in vitro and in vivo.
  Antimicrob Agents Chemother, 48, 1495-1502.  
15113911 J.Li, E.Quinlan, A.Mirza, and R.M.Iorio (2004).
Mutated form of the Newcastle disease virus hemagglutinin-neuraminidase interacts with the homologous fusion protein despite deficiencies in both receptor recognition and fusion promotion.
  J Virol, 78, 5299-5310.  
15466413 J.M.O'Leary, J.M.Hamilton, C.M.Deane, N.V.Valeyev, L.J.Sandell, and A.K.Downing (2004).
Solution structure and dynamics of a prototypical chordin-like cysteine-rich repeat (von Willebrand Factor type C module) from collagen IIA.
  J Biol Chem, 279, 53857-53866.
PDB code: 1u5m
14728685 L.Ferreira, E.Villar, and I.Muñoz-Barroso (2004).
Conformational changes of Newcastle disease virus envelope glycoproteins triggered by gangliosides.
  Eur J Biochem, 271, 581-588.  
15130470 M.F.Amaya, A.G.Watts, I.Damager, A.Wehenkel, T.Nguyen, A.Buschiazzo, G.Paris, A.C.Frasch, S.G.Withers, and P.M.Alzari (2004).
Structural insights into the catalytic mechanism of Trypanosoma cruzi trans-sialidase.
  Structure, 12, 775-784.
PDB codes: 1s0i 1s0j 1s0k 2ah2
15564499 M.Porotto, M.Murrell, O.Greengard, M.C.Lawrence, J.L.McKimm-Breschkin, and A.Moscona (2004).
Inhibition of parainfluenza virus type 3 and Newcastle disease virus hemagglutinin-neuraminidase receptor binding: effect of receptor avidity and steric hindrance at the inhibitor binding sites.
  J Virol, 78, 13911-13919.  
15308701 N.Massé, M.Ainouze, B.Néel, T.F.Wild, R.Buckland, and J.P.Langedijk (2004).
Measles virus (MV) hemagglutinin: evidence that attachment sites for MV receptors SLAM and CD46 overlap on the globular head.
  J Virol, 78, 9051-9063.  
15502328 S.Newstead, C.H.Chien, M.Taylor, and G.Taylor (2004).
Crystallization and atomic resolution X-ray diffraction of the catalytic domain of the large sialidase, nanI, from Clostridium perfringens.
  Acta Crystallogr D Biol Crystallogr, 60, 2063-2066.  
14671112 S.Vongpunsawad, N.Oezgun, W.Braun, and R.Cattaneo (2004).
Selectively receptor-blind measles viruses: Identification of residues necessary for SLAM- or CD46-induced fusion and their localization on a new hemagglutinin structural model.
  J Virol, 78, 302-313.  
15542686 T.L.Bousse, G.Taylor, S.Krishnamurthy, A.Portner, S.K.Samal, and T.Takimoto (2004).
Biological significance of the second receptor binding site of Newcastle disease virus hemagglutinin-neuraminidase protein.
  J Virol, 78, 13351-13355.  
15542657 V.R.Melanson, and R.M.Iorio (2004).
Amino acid substitutions in the F-specific domain in the stalk of the newcastle disease virus HN protein modulate fusion and interfere with its interaction with the F protein.
  J Virol, 78, 13053-13061.  
14730275 V.T.Peltola, and J.A.McCullers (2004).
Respiratory viruses predisposing to bacterial infections: role of neuraminidase.
  Pediatr Infect Dis J, 23, S87-S97.  
15016893 V.Zaitsev, M.von Itzstein, D.Groves, M.Kiefel, T.Takimoto, A.Portner, and G.Taylor (2004).
Second sialic acid binding site in Newcastle disease virus hemagglutinin-neuraminidase: implications for fusion.
  J Virol, 78, 3733-3741.
PDB codes: 1usr 1usx
15254162 V.von Messling, D.Milosevic, P.Devaux, and R.Cattaneo (2004).
Canine distemper virus and measles virus fusion glycoprotein trimers: partial membrane-proximal ectodomain cleavage enhances function.
  J Virol, 78, 7894-7903.  
15047833 Z.Huang, A.Panda, S.Elankumaran, D.Govindarajan, D.D.Rockemann, and S.K.Samal (2004).
The hemagglutinin-neuraminidase protein of Newcastle disease virus determines tropism and virulence.
  J Virol, 78, 4176-4184.  
14581458 C.J.Russell, K.L.Kantor, T.S.Jardetzky, and R.A.Lamb (2003).
A dual-functional paramyxovirus F protein regulatory switch segment: activation and membrane fusion.
  J Cell Biol, 163, 363-374.  
12768010 E.A.Corey, A.M.Mirza, E.Levandowsky, and R.M.Iorio (2003).
Fusion deficiency induced by mutations at the dimer interface in the Newcastle disease virus hemagglutinin-neuraminidase is due to a temperature-dependent defect in receptor binding.
  J Virol, 77, 6913-6922.  
14512552 K.A.Gravel, and T.G.Morrison (2003).
Interacting domains of the HN and F proteins of newcastle disease virus.
  J Virol, 77, 11040-11049.  
12477836 M.Murrell, M.Porotto, T.Weber, O.Greengard, and A.Moscona (2003).
Mutations in human parainfluenza virus type 3 hemagglutinin-neuraminidase causing increased receptor binding activity and resistance to the transition state sialic acid analog 4-GU-DANA (Zanamivir).
  J Virol, 77, 309-317.  
12610140 M.Porotto, M.Murrell, O.Greengard, and A.Moscona (2003).
Triggering of human parainfluenza virus 3 fusion protein (F) by the hemagglutinin-neuraminidase (HN) protein: an HN mutation diminishes the rate of F activation and fusion.
  J Virol, 77, 3647-3654.  
14557647 S.A.Rubin, G.Amexis, M.Pletnikov, Z.Li, J.Vanderzanden, J.Mauldin, C.Sauder, T.Malik, K.Chumakov, and K.M.Carbone (2003).
Changes in mumps virus gene sequence associated with variability in neurovirulent phenotype.
  J Virol, 77, 11616-11624.  
12419220 A.Buschiazzo, M.F.Amaya, M.L.Cremona, A.C.Frasch, and P.M.Alzari (2002).
The crystal structure and mode of action of trans-sialidase, a key enzyme in Trypanosoma cruzi pathogenesis.
  Mol Cell, 10, 757-768.
PDB codes: 1mr5 1ms0 1ms1 1ms3 1ms4 1ms5 1ms8 1ms9
12413546 A.Vasella, G.J.Davies, and M.Böhm (2002).
Glycosidase mechanisms.
  Curr Opin Chem Biol, 6, 619-629.  
12065582 C.Santiago, E.Björling, T.Stehle, and J.M.Casasnovas (2002).
Distinct kinetics for binding of the CD46 and SLAM receptors to overlapping sites in the measles virus hemagglutinin protein.
  J Biol Chem, 277, 32294-32301.  
11799177 H.Connaris, T.Takimoto, R.Russell, S.Crennell, I.Moustafa, A.Portner, and G.Taylor (2002).
Probing the sialic acid binding site of the hemagglutinin-neuraminidase of Newcastle disease virus: identification of key amino acids involved in cell binding, catalysis, and fusion.
  J Virol, 76, 1816-1824.  
12476442 J.J.Gorman, T.P.Wallis, and J.J.Pitt (2002).
Protein disulfide bond determination by mass spectrometry.
  Mass Spectrom Rev, 21, 183-216.  
12388678 K.N.Bossart, L.F.Wang, M.N.Flora, K.B.Chua, S.K.Lam, B.T.Eaton, and C.C.Broder (2002).
Membrane fusion tropism and heterotypic functional activities of the Nipah virus and Hendra virus envelope glycoproteins.
  J Virol, 76, 11186-11198.  
11864610 M.M.Mullen, K.M.Haan, R.Longnecker, and T.S.Jardetzky (2002).
Structure of the Epstein-Barr virus gp42 protein bound to the MHC class II receptor HLA-DR1.
  Mol Cell, 9, 375-385.
PDB code: 1kg0
12429084 P.M.Colman, and B.J.Smith (2002).
The trypanosomal trans-sialidase: two catalytic functions associated with one catalytic site.
  Structure, 10, 1466-1468.  
11867517 P.R.Dormitzer, Z.Y.Sun, G.Wagner, and S.C.Harrison (2002).
The rhesus rotavirus VP4 sialic acid binding domain has a galectin fold with a novel carbohydrate binding site.
  EMBO J, 21, 885-897.
PDB codes: 1kqr 1kri
12438628 T.Takimoto, G.L.Taylor, H.C.Connaris, S.J.Crennell, and A.Portner (2002).
Role of the hemagglutinin-neuraminidase protein in the mechanism of paramyxovirus-cell membrane fusion.
  J Virol, 76, 13028-13033.  
11483506 C.J.Russell, T.S.Jardetzky, and R.A.Lamb (2001).
Membrane fusion machines of paramyxoviruses: capture of intermediates of fusion.
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11711635 G.A.Prince, M.G.Ottolini, and A.Moscona (2001).
Contribution of the human parainfluenza virus type 3 HN-receptor interaction to pathogenesis in vivo.
  J Virol, 75, 12446-12451.  
11462020 M.Porotto, O.Greengard, N.Poltoratskaia, M.A.Horga, and A.Moscona (2001).
Human parainfluenza virus type 3 HN-receptor interaction: effect of 4-guanidino-Neu5Ac2en on a neuraminidase-deficient variant.
  J Virol, 75, 7481-7488.  
11413297 M.T.Murrell, M.Porotto, O.Greengard, N.Poltoratskaia, and A.Moscona (2001).
A single amino acid alteration in the human parainfluenza virus type 3 hemagglutinin-neuraminidase glycoprotein confers resistance to the inhibitory effects of zanamivir on receptor binding and neuraminidase activity.
  J Virol, 75, 6310-6320.  
11239770 T.G.Morrison (2001).
The three faces of paramyxovirus attachment proteins.
  Trends Microbiol, 9, 103-105.  
11312330 T.Suzuki, A.Portner, R.A.Scroggs, M.Uchikawa, N.Koyama, K.Matsuo, Y.Suzuki, and T.Takimoto (2001).
Receptor specificities of human respiroviruses.
  J Virol, 75, 4604-4613.  
11785761 Y.Bourne, and B.Henrissat (2001).
Glycoside hydrolases and glycosyltransferases: families and functional modules.
  Curr Opin Struct Biol, 11, 593-600.  
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