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PDBsum entry 1g2c
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Viral protein PDB id
1g2c

 

 

 

 

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Contents
Protein chains
50 a.a. *
40 a.a. *
36 a.a. *
37 a.a. *
50 a.a. *
40 a.a. *
47 a.a. *
50 a.a. *
38 a.a. *
Waters ×888
* Residue conservation analysis
PDB id:
1g2c
Name: Viral protein
Title: Human respiratory syncytial virus fusion protein core
Structure: Fusion protein (f). Chain: a, c, e, g, i, k, m, o, q, s, u, w. Fragment: residues 153-209, hrsv f1 heptad repeat. Synonym: cell fusion glycoprotein. Engineered: yes. Other_details: first heptad repeat. Fusion protein (f). Chain: b, d, f, h, j, l, n, p, r, t, v, x. Fragment: residues 476-520, hrsv f1 heptad repeat.
Source: Human respiratory syncytial virus. Organism_taxid: 11261. Strain: rss-2. Gene: hrsv f. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Hexamer (from PQS)
Resolution:
2.30Å     R-factor:   0.233     R-free:   0.286
Authors: X.Zhao,M.Singh,V.N.Malashkevich,P.S.Kim
Key ref:
X.Zhao et al. (2000). Structural characterization of the human respiratory syncytial virus fusion protein core. Proc Natl Acad Sci U S A, 97, 14172-14177. PubMed id: 11106388 DOI: 10.1073/pnas.260499197
Date:
18-Oct-00     Release date:   03-Jan-01    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P11209  (FUS_HRSVR) -  Fusion glycoprotein F0 from Human respiratory syncytial virus A (strain RSS-2)
Seq:
Struc: 		 
Seq:
Struc: 		574 a.a.
50 a.a.
Protein chain
Pfam   ArchSchema ?
P11209  (FUS_HRSVR) -  Fusion glycoprotein F0 from Human respiratory syncytial virus A (strain RSS-2)
Seq:
Struc: 		 
Seq:
Struc: 		574 a.a.
40 a.a.
Protein chains
Pfam   ArchSchema ?
P11209  (FUS_HRSVR) -  Fusion glycoprotein F0 from Human respiratory syncytial virus A (strain RSS-2)
Seq:
Struc: 		 
Seq:
Struc: 		574 a.a.
36 a.a.
Protein chains
Pfam   ArchSchema ?
P11209  (FUS_HRSVR) -  Fusion glycoprotein F0 from Human respiratory syncytial virus A (strain RSS-2)
Seq:
Struc: 		 
Seq:
Struc: 		574 a.a.
37 a.a.
Protein chains
Pfam   ArchSchema ?
P11209  (FUS_HRSVR) -  Fusion glycoprotein F0 from Human respiratory syncytial virus A (strain RSS-2)
Seq:
Struc: 		 
Seq:
Struc: 		574 a.a.
50 a.a.
Protein chain
Pfam   ArchSchema ?
P11209  (FUS_HRSVR) -  Fusion glycoprotein F0 from Human respiratory syncytial virus A (strain RSS-2)
Seq:
Struc: 		 
Seq:
Struc: 		574 a.a.
40 a.a.
Protein chain
Pfam   ArchSchema ?
P11209  (FUS_HRSVR) -  Fusion glycoprotein F0 from Human respiratory syncytial virus A (strain RSS-2)
Seq:
Struc: 		 
Seq:
Struc: 		574 a.a.
47 a.a.
Protein chains
Pfam   ArchSchema ?
P11209  (FUS_HRSVR) -  Fusion glycoprotein F0 from Human respiratory syncytial virus A (strain RSS-2)
Seq:
Struc: 		 
Seq:
Struc: 		574 a.a.
50 a.a.
Protein chains
Pfam   ArchSchema ?
P11209  (FUS_HRSVR) -  Fusion glycoprotein F0 from Human respiratory syncytial virus A (strain RSS-2)
Seq:
Struc: 		 
Seq:
Struc: 		574 a.a.
38 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1073/pnas.260499197 Proc Natl Acad Sci U S A 97:14172-14177 (2000)
PubMed id: 11106388  
 
 
Structural characterization of the human respiratory syncytial virus fusion protein core.
X.Zhao, M.Singh, V.N.Malashkevich, P.S.Kim.
 
  ABSTRACT  
 
Human respiratory syncytial virus (HRSV) is a major cause of a number of severe respiratory diseases, including bronchiolitis and pneumonia, in infants and young children. The HRSV F protein, a glycoprotein essential for viral entry, is a primary target for vaccine and drug development. Two heptad-repeat regions within the HRSV F sequence were predicted by the computer program learncoil-vmf. These regions are thought to form trimer-of-hairpins-like structures, similar to those found in the fusion proteins of several enveloped viruses. The hairpin structure likely brings the viral and cellular membranes into close apposition, thereby facilitating membrane fusion and subsequent viral entry. Here, we show that peptides, denoted HR-N and HR-C, corresponding to the heptad-repeat regions from the N-terminal and C-terminal segments of the HRSV F protein, respectively, form a stable alpha-helical trimer of heterodimers. The HRSV N/C complex was crystallized and its x-ray structure was determined at 2.3-A resolution. As anticipated, the complex is a six-helix bundle in which the HR-N peptides form a three-stranded, central coiled coil, and the HR-C peptides pack in an antiparallel manner into hydrophobic grooves on the coiled-coil surface. There is remarkable structural similarity between the HRSV N/C complex and the fusion protein core of other viruses, including HIV-1 gp41. In addition, earlier work has shown that HRSV HR-C peptides, like the HIV-1 gp41 C peptides, inhibit viral infection. Thus, drug discovery and vaccine development strategies aimed at inhibiting viral entry by blocking hairpin formation may be applied to the inhibition of HRSV.
 
  Selected figure(s)  
 
Figure 1.
Fig. 1. Schematic diagram of the HRSV F protein sequence. F1 and F2 are formed after proteolytic cleavage of the precursor F0. The signal peptide (SP), the cleavage site (CS), the putative fusion peptide (FP), the N-terminal HR (HR-N) region, the C-terminal HR (HR-C) region, and the transmembrane segment (TM) within the amino acid sequence of the recombinant recRSV-1 construct are indicated. The HR-N and HR-C regions predicted by LEARNCOIL-VMF are represented by shaded boxes. Protease-resistant fragments from trypsin (HRSV-N57 and HRSV-C45) and proteinase K (HRSV-N51 and HRSV-C39) cleavage are indicated. 		Figure 6.
Fig. 6. The cavity on the surface of the HRSV-N57 coiled coil. (A) A stereo view of interactions in the HRSV-N57 cavity. Two phenylalanine residues of HRSV-C45 (yellow) fit into the cavity formed by two neighboring HRSV-N57 peptides (blue). A prime symbol is used to distinguish residues from the two HRSV-N57 chains. Figure was prepared with MOLSCRIPT (45). (B) Comparison of cavity interactions of the HRSV and SV5 structures. The HRSV-N57 coiled coils, which superimpose closely with the SV5 N peptide coiled coils (21), are represented as a molecular surface (the most convex part shown in green and the most concave in gray). The HRSV-C45 (yellow) and SV5 C peptide (pink) helices are shown as ribbons with selected side chains that pack into the cavity. The relative shift of the C peptides is clearly visible. Figure was drawn with the program GRASP (46).
 
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19922971 A.S.Yunus, T.P.Jackson, K.Crisafi, I.Burimski, N.R.Kilgore, D.Zoumplis, G.P.Allaway, C.T.Wild, and K.Salzwedel (2010).
Elevated temperature triggers human respiratory syncytial virus F protein six-helix bundle formation.
  Virology, 396, 226-237.  
19966279 D.Roymans, H.L.De Bondt, E.Arnoult, P.Geluykens, T.Gevers, M.Van Ginderen, N.Verheyen, H.Kim, R.Willebrords, J.F.Bonfanti, W.Bruinzeel, M.D.Cummings, H.van Vlijmen, and K.Andries (2010).
Binding of a potent small-molecule inhibitor of six-helix bundle formation requires interactions with both heptad-repeats of the RSV fusion protein.
  Proc Natl Acad Sci U S A, 107, 308-313.
PDB code: 3kpe
20702638 E.C.Smith, and R.E.Dutch (2010).
Side chain packing below the fusion peptide strongly modulates triggering of the Hendra virus F protein.
  J Virol, 84, 10928-10932.  
20660316 G.H.Bird, N.Madani, A.F.Perry, A.M.Princiotto, J.G.Supko, X.He, E.Gavathiotis, J.G.Sodroski, and L.D.Walensky (2010).
Hydrocarbon double-stapling remedies the proteolytic instability of a lengthy peptide therapeutic.
  Proc Natl Acad Sci U S A, 107, 14093-14098.  
20519399 K.Huang, L.Incognito, X.Cheng, N.D.Ulbrandt, and H.Wu (2010).
Respiratory syncytial virus-neutralizing monoclonal antibodies motavizumab and palivizumab inhibit fusion.
  J Virol, 84, 8132-8140.  
20235830 K.M.Empey, R.S.Peebles, and J.K.Kolls (2010).
Pharmacologic advances in the treatment and prevention of respiratory syncytial virus.
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19906935 L.E.Luque, O.A.Bridges, J.N.Mason, K.L.Boyd, A.Portner, and C.J.Russell (2010).
Residues in the heptad repeat a region of the fusion protein modulate the virulence of Sendai virus in mice.
  J Virol, 84, 810-821.  
20534864 M.Magro, D.Andreu, P.Gómez-Puertas, J.A.Melero, and C.Palomo (2010).
Neutralization of human respiratory syncytial virus infectivity by antibodies and low-molecular-weight compounds targeted against the fusion glycoprotein.
  J Virol, 84, 7970-7982.  
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.
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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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  19954538 R.D.Cardin, F.J.Bravo, A.P.Sewell, J.Cummins, L.Flamand, J.M.Juteau, D.I.Bernstein, and A.Vaillant (2009).
Amphipathic DNA polymers exhibit antiviral activity against systemic Murine Cytomegalovirus infection.
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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.  
18094156 G.Long, X.Pan, and J.M.Vlak (2008).
Conserved leucines in N-terminal heptad repeat HR1 of envelope fusion protein F of group II nucleopolyhedroviruses are important for correct processing and essential for fusogenicity.
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18385247 J.Rawling, B.García-Barreno, and J.A.Melero (2008).
Insertion of the two cleavage sites of the respiratory syncytial virus fusion protein in Sendai virus fusion protein leads to enhanced cell-cell fusion and a decreased dependency on the HN attachment protein for activity.
  J Virol, 82, 5986-5998.  
18216117 K.Ludwig, B.Schade, C.Böttcher, T.Korte, N.Ohlwein, B.Baljinnyam, M.Veit, and A.Herrmann (2008).
Electron cryomicroscopy reveals different F1+F2 protein States in intact parainfluenza virions.
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19008400 N.D.Ulbrandt, H.Ji, N.K.Patel, A.S.Barnes, S.Wilson, P.A.Kiener, J.Suzich, and M.P.McCarthy (2008).
Identification of antibody neutralization epitopes on the fusion protein of human metapneumovirus.
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18417593 Z.N.Li, B.J.Lee, W.A.Langley, K.C.Bradley, R.J.Russell, and D.A.Steinhauer (2008).
Length requirements for membrane fusion of influenza virus hemagglutinin peptide linkers to transmembrane or fusion peptide domains.
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17957264 D.R.Beniac, S.L.Devarennes, A.Andonov, R.He, and T.F.Booth (2007).
Conformational Reorganization of the SARS Coronavirus Spike Following Receptor Binding: Implications for Membrane Fusion.
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17870467 R.A.Lamb, and T.S.Jardetzky (2007).
Structural basis of viral invasion: lessons from paramyxovirus F.
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17050595 R.L.Crim, S.A.Audet, S.A.Feldman, H.S.Mostowski, and J.A.Beeler (2007).
Identification of linear heparin-binding peptides derived from human respiratory syncytial virus fusion glycoprotein that inhibit infectivity.
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17457900 R.Marsh, A.Connor, E.Gias, and G.L.Toms (2007).
Increased susceptibility of human respiratory syncytial virus to neutralization by anti-fusion protein antibodies on adaptation to replication in cell culture.
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17035305 S.A.Miller, S.Tollefson, J.E.Crowe, J.V.Williams, and D.W.Wright (2007).
Examination of a fusogenic hexameric core from human metapneumovirus and identification of a potent synthetic peptide inhibitor from the heptad repeat 1 region.
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17287262 S.Seth, I.Skountzou, K.M.Gernert, and R.W.Compans (2007).
Fusogenic variants of a noncytopathic paramyxovirus.
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16569857 A.Vaillant, J.M.Juteau, H.Lu, S.Liu, C.Lackman-Smith, R.Ptak, and S.Jiang (2006).
Phosphorothioate oligonucleotides inhibit human immunodeficiency virus type 1 fusion by blocking gp41 core formation.
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16678421 C.J.Russell, and L.E.Luque (2006).
The structural basis of paramyxovirus invasion.
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16415028 J.Doyle, A.Prussia, L.K.White, A.Sun, D.C.Liotta, J.P.Snyder, R.W.Compans, and R.K.Plemper (2006).
Two domains that control prefusion stability and transport competence of the measles virus fusion protein.
  J Virol, 80, 1524-1536.  
16521129 K.S.Yeung, G.A.Yamanaka, and N.A.Meanwell (2006).
Severe acute respiratory syndrome coronavirus entry into host cells: Opportunities for therapeutic intervention.
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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.  
  16723026 N.D.Day, P.J.Branigan, C.Liu, L.L.Gutshall, J.Luo, J.A.Melero, R.T.Sarisky, and A.M.Del Vecchio (2006).
Contribution of cysteine residues in the extracellular domain of the F protein of human respiratory syncytial virus to its function.
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15650180 D.S.West, M.S.Sheehan, P.K.Segeleon, and R.E.Dutch (2005).
Role of the simian virus 5 fusion protein N-terminal coiled-coil domain in folding and promotion of membrane fusion.
  J Virol, 79, 1543-1551.  
15757395 G.F.Gao (2005).
Filling the hole: evidence of a small molecule binding to the fusion core pocket in human respiratory syncytial virus.
  Expert Opin Investig Drugs, 14, 195-197.  
15964978 H.S.Yin, R.G.Paterson, X.Wen, R.A.Lamb, and T.S.Jardetzky (2005).
Structure of the uncleaved ectodomain of the paramyxovirus (hPIV3) fusion protein.
  Proc Natl Acad Sci U S A, 102, 9288-9293.
PDB code: 1ztm
15917547 J.L.Douglas, M.L.Panis, E.Ho, K.Y.Lin, S.H.Krawczyk, D.M.Grant, R.Cai, S.Swaminathan, X.Chen, and T.Cihlar (2005).
Small molecules VP-14637 and JNJ-2408068 inhibit respiratory syncytial virus fusion by similar mechanisms.
  Antimicrob Agents Chemother, 49, 2460-2466.  
  16014172 P.J.Branigan, C.Liu, N.D.Day, L.L.Gutshall, R.T.Sarisky, and A.M.Del Vecchio (2005).
Use of a novel cell-based fusion reporter assay to explore the host range of human respiratory syncytial virus F protein.
  Virol J, 2, 54.  
16132115 S.C.Lai, P.C.Chong, C.T.Yeh, L.S.Liu, J.T.Jan, H.Y.Chi, H.W.Liu, A.Chen, and Y.C.Wang (2005).
Characterization of neutralizing monoclonal antibodies recognizing a 15-residues epitope on the spike protein HR2 region of severe acute respiratory syndrome coronavirus (SARS-CoV).
  J Biomed Sci, 12, 711-727.  
15827147 T.L.Gower, M.K.Pastey, M.E.Peeples, P.L.Collins, L.H.McCurdy, T.K.Hart, A.Guth, T.R.Johnson, and B.S.Graham (2005).
RhoA signaling is required for respiratory syncytial virus-induced syncytium formation and filamentous virion morphology.
  J Virol, 79, 5326-5336.  
15795264 W.Ou, and J.Silver (2005).
Inhibition of murine leukemia virus envelope protein (env) processing by intracellular expression of the env N-terminal heptad repeat region.
  J Virol, 79, 4782-4792.  
15368511 A.McGill, J.Greensill, R.Marsh, A.W.Craft, and G.L.Toms (2004).
Detection of human respiratory syncytial virus genotype specific antibody responses in infants.
  J Med Virol, 74, 492-498.  
15150417 B.J.Bosch, B.E.Martina, R.Van Der Zee, J.Lepault, B.J.Haijema, C.Versluis, A.J.Heck, R.De Groot, A.D.Osterhaus, and P.J.Rottier (2004).
Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides.
  Proc Natl Acad Sci U S A, 101, 8455-8460.  
15469910 C.Cianci, D.R.Langley, D.D.Dischino, Y.Sun, K.L.Yu, A.Stanley, J.Roach, Z.Li, R.Dalterio, R.Colonno, N.A.Meanwell, and M.Krystal (2004).
Targeting a binding pocket within the trimer-of-hairpins: small-molecule inhibition of viral fusion.
  Proc Natl Acad Sci U S A, 101, 15046-15051.  
14742189 C.Cianci, K.L.Yu, K.Combrink, N.Sin, B.Pearce, A.Wang, R.Civiello, S.Voss, G.Luo, K.Kadow, E.V.Genovesi, B.Venables, H.Gulgeze, A.Trehan, J.James, L.Lamb, I.Medina, J.Roach, Z.Yang, L.Zadjura, R.Colonno, J.Clark, N.Meanwell, and M.Krystal (2004).
Orally active fusion inhibitor of respiratory syncytial virus.
  Antimicrob Agents Chemother, 48, 413-422.  
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.  
15482225 J.L.Douglas (2004).
In search of a small-molecule inhibitor for respiratory syncytial virus.
  Expert Rev Anti Infect Ther, 2, 625-639.  
15161975 P.Ingallinella, E.Bianchi, M.Finotto, G.Cantoni, D.M.Eckert, V.M.Supekar, C.Bruckmann, A.Carfi, and A.Pessi (2004).
Structural characterization of the fusion-active complex of severe acute respiratory syndrome (SARS) coronavirus.
  Proc Natl Acad Sci U S A, 101, 8709-8714.  
15280460 S.Seth, A.L.Goodman, and R.W.Compans (2004).
Mutations in multiple domains activate paramyxovirus F protein-induced fusion.
  J Virol, 78, 8513-8523.  
15173835 S.Y.Seong, and P.Matzinger (2004).
Hydrophobicity: an ancient damage-associated molecular pattern that initiates innate immune responses.
  Nat Rev Immunol, 4, 469-478.  
15333939 X.Wang, Y.Xu, D.K.Cole, Z.Lou, Y.Liu, Z.Rao, M.Wang, and G.F.Gao (2004).
Biochemical, biophysical and preliminary X-ray crystallographic analyses of the fusion core of Sendai virus F protein.
  Acta Crystallogr D Biol Crystallogr, 60, 1632-1635.  
15583393 Y.Xu, N.Su, L.Qin, Z.Bai, G.F.Gao, and Z.Rao (2004).
Crystallization and preliminary crystallographic analysis of the heptad-repeat complex of SARS coronavirus spike protein.
  Acta Crystallogr D Biol Crystallogr, 60, 2377-2379.  
12885899 B.J.Bosch, R.van der Zee, C.A.de Haan, and P.J.Rottier (2003).
The coronavirus spike protein is a class I virus fusion protein: structural and functional characterization of the fusion core complex.
  J Virol, 77, 8801-8811.  
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.  
12692208 J.L.Douglas, M.L.Panis, E.Ho, K.Y.Lin, S.H.Krawczyk, D.M.Grant, R.Cai, S.Swaminathan, and T.Cihlar (2003).
Inhibition of respiratory syncytial virus fusion by the small molecule VP-14637 via specific interactions with F protein.
  J Virol, 77, 5054-5064.  
12595734 J.Zhu, Y.Ding, F.Gao, T.Wu, C.W.Zhang, P.Tien, Z.Rao, and G.F.Gao (2003).
Crystallization and preliminary X-ray crystallographic analysis of the trimer core from measles virus fusion protein.
  Acta Crystallogr D Biol Crystallogr, 59, 587-590.  
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.  
12881411 K.Ludwig, B.Baljinnyam, A.Herrmann, and C.Böttcher (2003).
The 3D structure of the fusion primed Sendai F-protein determined by electron cryomicroscopy.
  EMBO J, 22, 3761-3771.  
12948775 L.K.Tamm, J.Crane, and V.Kiessling (2003).
Membrane fusion: a structural perspective on the interplay of lipids and proteins.
  Curr Opin Struct Biol, 13, 453-466.  
14576104 P.J.Budge, J.Lebowitz, and B.S.Graham (2003).
Antiviral activity of RhoA-derived peptides against respiratory syncytial virus is dependent on formation of peptide dimers.
  Antimicrob Agents Chemother, 47, 3470-3477.  
12671653 P.M.Colman, and M.C.Lawrence (2003).
The structural biology of type I viral membrane fusion.
  Nat Rev Mol Cell Biol, 4, 309-319.  
12832792 P.Y.Li, J.Q.Zhu, B.L.Wu, F.Gao, P.Tien, Z.Rao, and G.F.Gao (2003).
Crystallization and preliminary X-ray diffraction analysis of post-fusion six-helix bundle core structure from Newcastle disease virus F protein.
  Acta Crystallogr D Biol Crystallogr, 59, 1296-1298.  
11850270 C.C.Huntley, W.J.Weiss, A.Gazumyan, A.Buklan, B.Feld, W.Hu, T.R.Jones, T.Murphy, A.A.Nikitenko, B.O'Hara, G.Prince, S.Quartuccio, Y.E.Raifeld, P.Wyde, and J.F.O'Connell (2002).
RFI-641, a potent respiratory syncytial virus inhibitor.
  Antimicrob Agents Chemother, 46, 841-847.  
12414953 C.M.Finnegan, W.Berg, G.K.Lewis, and A.L.DeVico (2002).
Antigenic properties of the human immunodeficiency virus transmembrane glycoprotein during cell-cell fusion.
  J Virol, 76, 12123-12134.  
11907215 F.A.Carneiro, M.L.Bianconi, G.Weissmüller, F.Stauffer, and A.T.Da Poian (2002).
Membrane recognition by vesicular stomatitis virus involves enthalpy-driven protein-lipid interactions.
  J Virol, 76, 3756-3764.  
12142481 J.M.Hogle (2002).
Poliovirus cell entry: common structural themes in viral cell entry pathways.
  Annu Rev Microbiol, 56, 677-702.  
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.  
12127571 K.San Román, E.Villar, and I.Muñoz-Barroso (2002).
Mode of action of two inhibitory peptides from heptad repeat domains of the fusion protein of Newcastle disease virus.
  Int J Biochem Cell Biol, 34, 1207-1220.  
12438588 L.W.McGinnes, K.Gravel, and T.G.Morrison (2002).
Newcastle disease virus HN protein alters the conformation of the F protein at cell surfaces.
  J Virol, 76, 12622-12633.  
12097599 R.J.Center, R.D.Leapman, J.Lebowitz, L.O.Arthur, P.L.Earl, and B.Moss (2002).
Oligomeric structure of the human immunodeficiency virus type 1 envelope protein on the virion surface.
  J Virol, 76, 7863-7867.  
11943545 S.G.Peisajovich, and Y.Shai (2002).
New insights into the mechanism of virus-induced membrane fusion.
  Trends Biochem Sci, 27, 183-190.  
11413331 A.L.Maerz, H.E.Drummer, K.A.Wilson, and P.Poumbourios (2001).
Functional analysis of the disulfide-bonded loop/chain reversal region of human immunodeficiency virus type 1 gp41 reveals a critical role in gp120-gp41 association.
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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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11395423 D.M.Eckert, and P.S.Kim (2001).
Mechanisms of viral membrane fusion and its inhibition.
  Annu Rev Biochem, 70, 777-810.  
11500371 K.J.Cross, S.A.Wharton, J.J.Skehel, D.C.Wiley, and D.A.Steinhauer (2001).
Studies on influenza haemagglutinin fusion peptide mutants generated by reverse genetics.
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11493675 L.González-Reyes, M.B.Ruiz-Argüello, B.García-Barreno, L.Calder, J.A.López, J.P.Albar, J.J.Skehel, D.C.Wiley, and J.A.Melero (2001).
Cleavage of the human respiratory syncytial virus fusion protein at two distinct sites is required for activation of membrane fusion.
  Proc Natl Acad Sci U S A, 98, 9859-9864.  
11445467 M.A.Walker (2001).
Novel antiviral molecules.
  Drug Discov Today, 6, 747-749.  
11533163 M.Tsurudome, M.Ito, M.Nishio, M.Kawano, H.Komada, and Y.Ito (2001).
Hemagglutinin-neuraminidase-independent fusion activity of simian virus 5 fusion (F) protein: difference in conformation between fusogenic and nonfusogenic F proteins on the cell surface.
  J Virol, 75, 8999-9009.  
11752436 R.J.Center, P.Schuck, R.D.Leapman, L.O.Arthur, P.L.Earl, B.Moss, and J.Lebowitz (2001).
Oligomeric structure of virion-associated and soluble forms of the simian immunodeficiency virus envelope protein in the prefusion activated conformation.
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11483738 T.A.Sergel, L.W.McGinnes, and T.G.Morrison (2001).
Mutations in the fusion peptide and adjacent heptad repeat inhibit folding or activity of the Newcastle disease virus fusion protein.
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11447278 V.N.Malashkevich, M.Singh, and P.S.Kim (2001).
The trimer-of-hairpins motif in membrane fusion: Visna virus.
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PDB code: 1jek
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 code is shown on the right.

 

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