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PDBsum entry 1d3e

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protein links
Virus/receptor PDB id
1d3e
Contents
Protein chains
185 a.a.* *
285 a.a.* *
252 a.a.* *
238 a.a.* *
29 a.a.* *
* Residue conservation analysis
* C-alpha coords only
PDB id:
1d3e
Name: Virus/receptor
Title: Cryo-em structure of human rhinovirus 16 (hrv16) complexed with a two- domain fragment of its cellular receptor, intercellular adhesion molecule-1 (d1d2-icam-1). Implications for virus-receptor interactions. Alpha carbons only
Structure: Protein (intercellular adhesion molecule-1). Chain: i. Fragment: first two domains, residues 1-185. Synonym: d1d2-icam-1. Protein (rhinovirus 16 coat protein vp1). Chain: 1. Synonym: hrv16 vp1. Protein (rhinovirus 16 coat protein vp2). Chain: 2.
Source: Fragment: 1 - 185. Homo sapiens. Human. Organism_taxid: 9606. Human rhinovirus sp.. Organism_taxid: 169066. Strain: serotype 16. Strain: serotype 16
Authors: J.Bella,M.G.Rossmann
Key ref:
P.R.Kolatkar et al. (1999). Structural studies of two rhinovirus serotypes complexed with fragments of their cellular receptor. EMBO J, 18, 6249-6259. PubMed id: 10562537 DOI: 10.1093/emboj/18.22.6249
Date:
29-Sep-99     Release date:   19-Jan-00    
 Headers
 References

Protein chain
P05362  (ICAM1_HUMAN) -  Intercellular adhesion molecule 1 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
532 a.a.
185 a.a.
Protein chain
Q82122  (POLG_HRV16) -  Genome polyprotein from Human rhinovirus 16
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
2153 a.a.
285 a.a.*
Protein chain
Q82122  (POLG_HRV16) -  Genome polyprotein from Human rhinovirus 16
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
2153 a.a.
252 a.a.*
Protein chain
Q82122  (POLG_HRV16) -  Genome polyprotein from Human rhinovirus 16
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
2153 a.a.
238 a.a.
Protein chain
Q82122  (POLG_HRV16) -  Genome polyprotein from Human rhinovirus 16
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
2153 a.a.
29 a.a.
Key:    Secondary structure
* PDB and UniProt seqs differ at 7 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class 2: Chains 1, 2, 3, 4: E.C.2.7.7.48  - RNA-directed Rna polymerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate
RNA(n)
+ ribonucleoside 5'-triphosphate
= RNA(n+1)
+ diphosphate
   Enzyme class 3: Chains 1, 2, 3, 4: E.C.3.4.22.28  - picornain 3C.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
   Enzyme class 4: Chains 1, 2, 3, 4: E.C.3.4.22.29  - picornain 2A.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
   Enzyme class 5: Chains 1, 2, 3, 4: E.C.3.6.1.15  - nucleoside-triphosphate phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + phosphate + H+
ribonucleoside 5'-triphosphate
+ H2O
= ribonucleoside 5'-diphosphate
+ phosphate
+ H(+)
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1093/emboj/18.22.6249 EMBO J 18:6249-6259 (1999)
PubMed id: 10562537  
 
 
Structural studies of two rhinovirus serotypes complexed with fragments of their cellular receptor.
P.R.Kolatkar, J.Bella, N.H.Olson, C.M.Bator, T.S.Baker, M.G.Rossmann.
 
  ABSTRACT  
 
Two human rhinovirus serotypes complexed with two- and five-domain soluble fragments of the cellular receptor, intercellular adhesion molecule-1, have been investigated by X-ray crystallographic analyses of the individual components and by cryo-electron microscopy of the complexes. The three-dimensional image reconstructions provide a molecular envelope within which the crystal structures of the viruses and the receptor fragments can be positioned with accuracy. The N-terminal domain of the receptor binds to the rhinovirus 'canyon' surrounding the icosahedral 5-fold axes. Fitting of molecular models into the image reconstruction density identified the residues on the virus that interact with those on the receptor surface, demonstrating complementarity of the electrostatic patterns for the tip of the N-terminal receptor domain and the floor of the canyon. The complexes seen in the image reconstructions probably represent the first stage of a multistep binding process. A mechanism is proposed for the subsequent viral uncoating process.
 
  Selected figure(s)  
 
Figure 5.
Figure 5 Roadmap representation (Chapman, 1993) showing the amino acids within the ICAM-1 footprint (thick outline) on the surface of (A) HRV16 and (B) HRV14. The figure shows one icosahedral asymmetric unit with a 5-fold axis at the top and 3-fold axes to the left and right at the bottom. Residues closer than 145 Å to the viral center, shaded in gray, outline the central and deepest region of the canyon.
Figure 6.
Figure 6 Stereo representations of electrostatic charge distribution in the canyon region of HRV16 (top), HRV14 (bottom) and the tip of ICAM-1. Charge distributions are represented by the usual colors. Residues that show charge complementarity are indicated and connected with dashed lines.
 
  The above figures are reprinted from an Open Access publication published by Macmillan Publishers Ltd: EMBO J (1999, 18, 6249-6259) copyright 1999.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
22472617 J.M.Hogle (2012).
A 3D framework for understanding enterovirus 71.
  Nat Struct Mol Biol, 19, 367-368.  
19714577 J.M.Rollinger, and M.Schmidtke (2011).
The human rhinovirus: human-pathological impact, mechanisms of antirhinoviral agents, and strategies for their discovery.
  Med Res Rev, 31, 42-92.  
21390226 L.B.Ochola, B.R.Siddondo, H.Ocholla, S.Nkya, E.N.Kimani, T.N.Williams, J.O.Makale, A.Liljander, B.C.Urban, P.C.Bull, T.Szestak, K.Marsh, and A.G.Craig (2011).
Specific receptor usage in Plasmodium falciparum cytoadherence is associated with disease outcome.
  PLoS One, 6, e14741.  
20554778 J.Seitsonen, P.Susi, O.Heikkilä, R.S.Sinkovits, P.Laurinmäki, T.Hyypiä, and S.J.Butcher (2010).
Interaction of alphaVbeta3 and alphaVbeta6 integrins with human parechovirus 1.
  J Virol, 84, 8509-8519.  
20629045 R.Fuchs, and D.Blaas (2010).
Uncoating of human rhinoviruses.
  Rev Med Virol, 20, 281-297.  
19925687 J.Y.Lin, T.C.Chen, K.F.Weng, S.C.Chang, L.L.Chen, and S.R.Shih (2009).
Viral and host proteins involved in picornavirus life cycle.
  J Biomed Sci, 16, 103.  
19182223 N.Lewis-Rogers, M.L.Bendall, and K.A.Crandall (2009).
Phylogenetic relationships and molecular adaptation dynamics of human rhinoviruses.
  Mol Biol Evol, 26, 969-981.  
19264616 S.Blomqvist, C.Savolainen-Kopra, A.Paananen, T.Hovi, and M.Roivainen (2009).
Molecular characterization of human rhinovirus field strains isolated during surveillance of enteroviruses.
  J Gen Virol, 90, 1371-1381.  
19726496 S.Lindert, M.Silvestry, T.M.Mullen, G.R.Nemerow, and P.L.Stewart (2009).
Cryo-electron microscopy structure of an adenovirus-integrin complex indicates conformational changes in both penton base and integrin.
  J Virol, 83, 11491-11501.  
18442921 D.Bubeck, D.J.Filman, M.Kuzmin, S.D.Fuller, and J.M.Hogle (2008).
Post-imaging fiducial markers aid in the orientation determination of complexes with mixed or unknown symmetry.
  J Struct Biol, 162, 480-490.  
18382652 P.McErlean, L.A.Shackelton, E.Andrews, D.R.Webster, S.B.Lambert, M.D.Nissen, T.P.Sloots, and I.M.Mackay (2008).
Distinguishing molecular features and clinical characteristics of a putative new rhinovirus species, human rhinovirus C (HRV C).
  PLoS ONE, 3, e1847.  
19011098 P.Zhang, S.Mueller, M.C.Morais, C.M.Bator, V.D.Bowman, S.Hafenstein, E.Wimmer, and M.G.Rossmann (2008).
Crystal structure of CD155 and electron microscopic studies of its complexes with polioviruses.
  Proc Natl Acad Sci U S A, 105, 18284-18289.
PDB codes: 3eow 3epc 3epd 3epf 3uro
17116403 C.Xiao, and M.G.Rossmann (2007).
Interpretation of electron density with stereographic roadmap projections.
  J Struct Biol, 158, 182-187.  
17164521 M.G.Rossmann, F.Arisaka, A.J.Battisti, V.D.Bowman, P.R.Chipman, A.Fokine, S.Hafenstein, S.Kanamaru, V.A.Kostyuchenko, V.V.Mesyanzhinov, M.M.Shneider, M.C.Morais, P.G.Leiman, L.M.Palermo, C.R.Parrish, and C.Xiao (2007).
From structure of the complex to understanding of the biology.
  Acta Crystallogr D Biol Crystallogr, 63, 9.  
17537857 M.S.Kim, and V.R.Racaniello (2007).
Enterovirus 70 receptor utilization is controlled by capsid residues that also regulate host range and cytopathogenicity.
  J Virol, 81, 8648-8655.  
17804498 S.Hafenstein, V.D.Bowman, P.R.Chipman, C.M.Bator Kelly, F.Lin, M.E.Medof, and M.G.Rossmann (2007).
Interaction of decay-accelerating factor with coxsackievirus B3.
  J Virol, 81, 12927-12935.
PDB codes: 2qzd 2qzf 2qzh
16272562 D.M.Pettigrew, D.T.Williams, D.Kerrigan, D.J.Evans, S.M.Lea, and D.Bhella (2006).
Structural and functional insights into the interaction of echoviruses and decay-accelerating factor.
  J Biol Chem, 281, 5169-5177.
PDB code: 2c8i
15965485 D.Bubeck, D.J.Filman, and J.M.Hogle (2005).
Cryo-electron microscopy reconstruction of a poliovirus-receptor-membrane complex.
  Nat Struct Mol Biol, 12, 615-618.  
15919927 D.Bubeck, D.J.Filman, N.Cheng, A.C.Steven, J.M.Hogle, and D.M.Belnap (2005).
The structure of the poliovirus 135S cell entry intermediate at 10-angstrom resolution reveals the location of an externalized polypeptide that binds to membranes.
  J Virol, 79, 7745-7755.
PDB code: 1xyr
15545280 D.Jiménez, P.Roda-Navarro, T.A.Springer, and J.M.Casasnovas (2005).
Contribution of N-linked glycans to the conformation and function of intercellular adhesion molecules (ICAMs).
  J Biol Chem, 280, 5854-5861.  
15883190 L.Wang, and D.L.Smith (2005).
Capsid structure and dynamics of a human rhinovirus probed by hydrogen exchange mass spectrometry.
  Protein Sci, 14, 1661-1672.  
15766536 M.G.Rossmann, M.C.Morais, P.G.Leiman, and W.Zhang (2005).
Combining X-ray crystallography and electron microscopy.
  Structure, 13, 355-362.  
15353596 A.T.Dufresne, and M.Gromeier (2004).
A nonpolio enterovirus with respiratory tropism causes poliomyelitis in intercellular adhesion molecule 1 transgenic mice.
  Proc Natl Acad Sci U S A, 101, 13636-13641.  
15331736 C.Xiao, T.J.Tuthill, C.M.Bator Kelly, L.J.Challinor, P.R.Chipman, R.A.Killington, D.J.Rowlands, A.Craig, and M.G.Rossmann (2004).
Discrimination among rhinovirus serotypes for a variant ICAM-1 receptor molecule.
  J Virol, 78, 10034-10044.  
14634014 D.Bhella, I.G.Goodfellow, P.Roversi, D.Pettigrew, Y.Chaudhry, D.J.Evans, and S.M.Lea (2004).
The structure of echovirus type 12 bound to a two-domain fragment of its cellular attachment protein decay-accelerating factor (CD 55).
  J Biol Chem, 279, 8325-8332.
PDB code: 1upn
14990711 E.A.Hewat, and D.Blaas (2004).
Cryoelectron microscopy analysis of the structural changes associated with human rhinovirus type 14 uncoating.
  J Virol, 78, 2935-2942.  
15507647 E.S.Johansson, L.Xing, R.H.Cheng, and D.R.Shafren (2004).
Enhanced cellular receptor usage by a bioselected variant of coxsackievirus a21.
  J Virol, 78, 12603-12612.  
15331710 H.Duque, M.LaRocco, W.T.Golde, and B.Baxt (2004).
Interactions of foot-and-mouth disease virus with soluble bovine alphaVbeta3 and alphaVbeta6 integrins.
  J Virol, 78, 9773-9781.  
15084510 M.J.Grubman, and B.Baxt (2004).
Foot-and-mouth disease.
  Clin Microbiol Rev, 17, 465-493.  
14763979 M.T.Tse, K.Chakrabarti, C.Gray, C.E.Chitnis, and A.Craig (2004).
Divergent binding sites on intercellular adhesion molecule-1 (ICAM-1) for variant Plasmodium falciparum isolates.
  Mol Microbiol, 51, 1039-1049.  
15114337 S.C.Blacklow (2004).
Catching the common cold.
  Nat Struct Mol Biol, 11, 388-390.  
15452226 Y.Zhang, A.A.Simpson, R.M.Ledford, C.M.Bator, S.Chakravarty, G.A.Skochko, T.M.Demenczuk, A.Watanyar, D.C.Pevear, and M.G.Rossmann (2004).
Structural and virological studies of the stages of virus replication that are affected by antirhinovirus compounds.
  J Virol, 78, 11061-11069.
PDB codes: 1na1 1ncq 1ncr 1nd2 1nd3
14646061 A.A.Simpson, N.Nandhagopal, J.L.Van Etten, and M.G.Rossmann (2003).
Structural analyses of Phycodnaviridae and Iridoviridae.
  Acta Crystallogr D Biol Crystallogr, 59, 2053-2059.  
12871973 A.P.Mould, E.J.Symonds, P.A.Buckley, J.G.Grossmann, P.A.McEwan, S.J.Barton, J.A.Askari, S.E.Craig, J.Bella, and M.J.Humphries (2003).
Structure of an integrin-ligand complex deduced from solution x-ray scattering and site-directed mutagenesis.
  J Biol Chem, 278, 39993-39999.  
12692248 E.E.Fry, N.J.Knowles, J.W.Newman, G.Wilsden, Z.Rao, A.M.King, and D.I.Stuart (2003).
Crystal structure of Swine vesicular disease virus and implications for host adaptation.
  J Virol, 77, 5475-5486.
PDB code: 1oop
12857919 E.Neumann, R.Moser, L.Snyers, D.Blaas, and E.A.Hewat (2003).
A cellular receptor of human rhinovirus type 2, the very-low-density lipoprotein receptor, binds to two neighboring proteins of the viral capsid.
  J Virol, 77, 8504-8511.  
14581535 G.Nurani, B.Lindqvist, and J.M.Casasnovas (2003).
Receptor priming of major group human rhinoviruses for uncoating and entry at mild low-pH environments.
  J Virol, 77, 11985-11991.  
12966102 J.C.Forrest, J.A.Campbell, P.Schelling, T.Stehle, and T.S.Dermody (2003).
Structure-function analysis of reovirus binding to junctional adhesion molecule 1. Implications for the mechanism of reovirus attachment.
  J Biol Chem, 278, 48434-48444.  
12885341 L.Vijgen, M.Van Essche, and M.Van Ranst (2003).
Absence of the Kilifi mutation in the rhinovirus-binding domain of ICAM-1 in a Caucasian population.
  Genet Test, 7, 159-161.  
12743267 L.Xing, J.M.Casasnovas, and R.H.Cheng (2003).
Structural analysis of human rhinovirus complexed with ICAM-1 reveals the dynamics of receptor-mediated virus uncoating.
  J Virol, 77, 6101-6107.  
12511869 M.Bomsel, and A.Alfsen (2003).
Entry of viruses through the epithelial barrier: pathogenic trickery.
  Nat Rev Mol Cell Biol, 4, 57-68.  
12692239 M.Brabec, G.Baravalle, D.Blaas, and R.Fuchs (2003).
Conformational changes, plasma membrane penetration, and infection by human rhinovirus type 2: role of receptors and low pH.
  J Virol, 77, 5370-5377.  
12768011 M.Vlasak, S.Blomqvist, T.Hovi, E.Hewat, and D.Blaas (2003).
Sequence and structure of human rhinoviruses reveal the basis of receptor discrimination.
  J Virol, 77, 6923-6930.  
12941886 N.Verdaguer, M.A.Jimenez-Clavero, I.Fita, and V.Ley (2003).
Structure of swine vesicular disease virus: mapping of changes occurring during adaptation of human coxsackie B5 virus to infect swine.
  J Virol, 77, 9780-9789.
PDB code: 1mqt
12663789 Y.He, S.Mueller, P.R.Chipman, C.M.Bator, X.Peng, V.D.Bowman, S.Mukhopadhyay, E.Wimmer, R.J.Kuhn, and M.G.Rossmann (2003).
Complexes of poliovirus serotypes with their common cellular receptor, CD155.
  J Virol, 77, 4827-4835.
PDB code: 1nn8
12186914 A.D.Stuart, H.E.Eustace, T.A.McKee, and T.D.Brown (2002).
A novel cell entry pathway for a DAF-using human enterovirus is dependent on lipid rafts.
  J Virol, 76, 9307-9322.  
12097583 A.D.Stuart, T.A.McKee, P.A.Williams, C.Harley, S.Shen, D.I.Stuart, T.D.Brown, and S.M.Lea (2002).
Determination of the structure of a decay accelerating factor-binding clinical isolate of echovirus 11 allows mapping of mutants with altered receptor requirements for infection.
  J Virol, 76, 7694-7704.
PDB code: 1h8t
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.  
12191477 E.A.Hewat, E.Neumann, and D.Blaas (2002).
The concerted conformational changes during human rhinovirus 2 uncoating.
  Mol Cell, 10, 317-326.  
12142481 J.M.Hogle (2002).
Poliovirus cell entry: common structural themes in viral cell entry pathways.
  Annu Rev Microbiol, 56, 677-702.  
11893508 J.Wang (2002).
Protein recognition by cell surface receptors: physiological receptors versus virus interactions.
  Trends Biochem Sci, 27, 122-126.  
11980704 K.Tan, B.D.Zelus, R.Meijers, J.H.Liu, J.M.Bergelson, N.Duke, R.Zhang, A.Joachimiak, K.V.Holmes, and J.H.Wang (2002).
Crystal structure of murine sCEACAM1a[1,4]: a coronavirus receptor in the CEA family.
  EMBO J, 21, 2076-2086.
PDB code: 1l6z
12110211 M.G.Rossmann, Y.He, and R.J.Kuhn (2002).
Picornavirus-receptor interactions.
  Trends Microbiol, 10, 324-331.  
12072496 M.Reithmayer, A.Reischl, L.Snyers, and D.Blaas (2002).
Species-specific receptor recognition by a minor-group human rhinovirus (HRV): HRV serotype 1A distinguishes between the murine and the human low-density lipoprotein receptor.
  J Virol, 76, 6957-6965.  
12119400 Y.He, F.Lin, P.R.Chipman, C.M.Bator, T.S.Baker, M.Shoham, R.J.Kuhn, M.E.Medof, and M.G.Rossmann (2002).
Structure of decay-accelerating factor bound to echovirus 7: a virus-receptor complex.
  Proc Natl Acad Sci U S A, 99, 10325-10329.
PDB code: 1m11
11533194 A.Reischl, M.Reithmayer, G.Winsauer, R.Moser, I.Gösler, and D.Blaas (2001).
Viral evolution toward change in receptor usage: adaptation of a major group human rhinovirus to grow in ICAM-1-negative cells.
  J Virol, 75, 9312-9319.  
11160747 C.Xiao, C.M.Bator, V.D.Bowman, E.Rieder, Y.He, B.Hébert, J.Bella, T.S.Baker, E.Wimmer, R.J.Kuhn, and M.G.Rossmann (2001).
Interaction of coxsackievirus A21 with its cellular receptor, ICAM-1.
  J Virol, 75, 2444-2451.  
11602751 M.E.Bloom, S.M.Best, S.F.Hayes, R.D.Wells, J.B.Wolfinbarger, R.McKenna, and M.Agbandje-McKenna (2001).
Identification of aleutian mink disease parvovirus capsid sequences mediating antibody-dependent enhancement of infection, virus neutralization, and immune complex formation.
  J Virol, 75, 11116-11127.  
11573093 Y.He, P.R.Chipman, J.Howitt, C.M.Bator, M.A.Whitt, T.S.Baker, R.J.Kuhn, C.W.Anderson, P.Freimuth, and M.G.Rossmann (2001).
Interaction of coxsackievirus B3 with the full length coxsackievirus-adenovirus receptor.
  Nat Struct Biol, 8, 874-878.
PDB code: 1jew
10998630 A.M.Roseman (2000).
Docking structures of domains into maps from cryo-electron microscopy using local correlation.
  Acta Crystallogr D Biol Crystallogr, 56, 1332-1340.  
10618373 D.M.Belnap, B.M.McDermott, D.J.Filman, N.Cheng, B.L.Trus, H.J.Zuccola, V.R.Racaniello, J.M.Hogle, and A.C.Steven (2000).
Three-dimensional structure of poliovirus receptor bound to poliovirus.
  Proc Natl Acad Sci U S A, 97, 73-78.  
11101504 E.A.Hewat, E.Neumann, J.F.Conway, R.Moser, B.Ronacher, T.C.Marlovits, and D.Blaas (2000).
The cellular receptor to human rhinovirus 2 binds around the 5-fold axis and not in the canyon: a structural view.
  EMBO J, 19, 6317-6325.  
10998624 E.J.Mancini, and S.D.Fuller (2000).
Supplanting crystallography or supplementing microscopy? A combined approach to the study of an enveloped virus.
  Acta Crystallogr D Biol Crystallogr, 56, 1278-1287.  
10838577 J.Bella, and M.G.Rossmann (2000).
The dynamics of receptor recognition by human rhinoviruses: response
  Trends Microbiol, 8, 254.  
10838576 J.M.Casasnovas (2000).
The dynamics of receptor recognition by human rhinoviruses.
  Trends Microbiol, 8, 251-254.  
10998631 M.G.Rossmann (2000).
Fitting atomic models into electron-microscopy maps.
  Acta Crystallogr D Biol Crystallogr, 56, 1341-1349.  
11188697 P.D.Kwong, R.Wyatt, S.Majeed, J.Robinson, R.W.Sweet, J.Sodroski, and W.A.Hendrickson (2000).
Structures of HIV-1 gp120 envelope glycoproteins from laboratory-adapted and primary isolates.
  Structure, 8, 1329-1339.
PDB codes: 1g9m 1g9n
10618374 Y.He, V.D.Bowman, S.Mueller, C.M.Bator, J.Bella, X.Peng, T.S.Baker, E.Wimmer, R.J.Kuhn, and M.G.Rossmann (2000).
Interaction of the poliovirus receptor with poliovirus.
  Proc Natl Acad Sci U S A, 97, 79-84.
PDB code: 1dgi
11042462 Y.Tao, and W.Zhang (2000).
Recent developments in cryo-electron microscopy reconstruction of single particles.
  Curr Opin Struct Biol, 10, 616-622.  
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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