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PDBsum entry 2ny3

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protein ligands Protein-protein interface(s) links
Viral protein/immune system PDB id
2ny3
Jmol
Contents
Protein chains
305 a.a. *
181 a.a. *
214 a.a. *
223 a.a. *
Ligands
NAG ×13
SUC
Waters ×665
* Residue conservation analysis
PDB id:
2ny3
Name: Viral protein/immune system
Title: HIV-1 gp120 envelope glycoprotein (k231c, t257s, e267c, s334 complexed with cd4 and antibody 17b
Structure: Envelope glycoprotein gp120. Chain: a. Fragment: core. Engineered: yes. Mutation: yes. T-cell surface glycoprotein cd4. Chain: b. Fragment: d1d2, n-terminal two domain fragment. Synonym: t-cell surface antigen t4/leu-3.
Source: Human immunodeficiency virus 1. Organism_taxid: 11676. Strain: hxbc2. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: embryonic cell line 293. Expression_system_organ: kidney. Homo sapiens. Human.
Resolution:
2.00Å     R-factor:   0.205     R-free:   0.243
Authors: T.Zhou,L.Xu,B.Dey,A.J.Hessell,D.Van Ryk,S.H.Xiang,X.Yang,M.Y M.B.Zwick,J.Arthos,D.R.Burton,D.S.Dimitrov,J.Sodroski,R.Wya G.J.Nabel,P.D.Kwong
Key ref:
T.Zhou et al. (2007). Structural definition of a conserved neutralization epitope on HIV-1 gp120. Nature, 445, 732-737. PubMed id: 17301785 DOI: 10.1038/nature05580
Date:
20-Nov-06     Release date:   06-Feb-07    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q993A8  (Q993A8_9HIV1) -  Envelope glycoprotein (Fragment)
Seq:
Struc:
 
Seq:
Struc:
588 a.a.
305 a.a.*
Protein chain
Pfam   ArchSchema ?
P01730  (CD4_HUMAN) -  T-cell surface glycoprotein CD4
Seq:
Struc:
458 a.a.
181 a.a.
Protein chain
Pfam   ArchSchema ?
Q6P5S8  (Q6P5S8_HUMAN) -  IGK@ protein
Seq:
Struc:
236 a.a.
214 a.a.*
Protein chain
Pfam   ArchSchema ?
Q6N030  (Q6N030_HUMAN) -  Putative uncharacterized protein DKFZp686I15212
Seq:
Struc:
 
Seq:
Struc:
518 a.a.
223 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 94 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     viral envelope   2 terms 
  Biological process     cell adhesion   1 term 

 

 
DOI no: 10.1038/nature05580 Nature 445:732-737 (2007)
PubMed id: 17301785  
 
 
Structural definition of a conserved neutralization epitope on HIV-1 gp120.
T.Zhou, L.Xu, B.Dey, A.J.Hessell, D.Van Ryk, S.H.Xiang, X.Yang, M.Y.Zhang, M.B.Zwick, J.Arthos, D.R.Burton, D.S.Dimitrov, J.Sodroski, R.Wyatt, G.J.Nabel, P.D.Kwong.
 
  ABSTRACT  
 
The remarkable diversity, glycosylation and conformational flexibility of the human immunodeficiency virus type 1 (HIV-1) envelope (Env), including substantial rearrangement of the gp120 glycoprotein upon binding the CD4 receptor, allow it to evade antibody-mediated neutralization. Despite this complexity, the HIV-1 Env must retain conserved determinants that mediate CD4 binding. To evaluate how these determinants might provide opportunities for antibody recognition, we created variants of gp120 stabilized in the CD4-bound state, assessed binding of CD4 and of receptor-binding-site antibodies, and determined the structure at 2.3 A resolution of the broadly neutralizing antibody b12 in complex with gp120. b12 binds to a conformationally invariant surface that overlaps a distinct subset of the CD4-binding site. This surface is involved in the metastable attachment of CD4, before the gp120 rearrangement required for stable engagement. A site of vulnerability, related to a functional requirement for efficient association with CD4, can therefore be targeted by antibody to neutralize HIV-1.
 
  Selected figure(s)  
 
Figure 2.
Figure 2: Conformational states of gp120. The unliganded, b12- and CD4-bound conformations of gp120 are depicted, with polypeptide in ribbon representation and disordered regions as dashed lines. Inner domains are grey, outer domains are red and regions that in the CD4-bound state correspond to the bridging sheet are blue. Both b12- and CD4-bound conformations are of the Ds12 F123 variant of HIV-1, whereas the unliganded structure is of simian immunodeficiency virus (SIV). Comparison of these three gp120 conformations highlights not only the structural plasticity of the inner domain and bridging sheet, but also the conformational stability of the outer domain.
Figure 4.
Figure 4: Structural definition of a conformationally invariant, antibody-accessible portion of the CD4-binding site. The b12- and CD4-bound conformations of gp120 are shown in ribbon representation, after superposition of outer domains (red). A semitransparent molecular surface shows the contact surfaces of b12 (green) and CD4 (yellow). Subsets of these surfaces, corresponding to regions of conformational flexibility (for example, of the inner domain (grey) or bridging sheet (blue)), are delineated, as are regions of b12 contact outside of the conserved CD4-binding site. As can be seen, functional analysis serves to transcend the particulars of b12 binding, whereas antibody defines accessibility. Although we have formally shown only the b12 contact surface to be accessible in the context of a functional viral spike, the highly effective neutralization of D1D2-Ig tp and the kinetics of its association with both core and OD1 variants of gp120 suggest that the CD4-binding surface on the outer domain is accessible.
 
  The above figures are reprinted by permission from Macmillan Publishers Ltd: Nature (2007, 445, 732-737) copyright 2007.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
23007571 P.C.Wilson, and S.F.Andrews (2012).
Tools to therapeutically harness the human antibody response.
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Subunit organization of the membrane-bound HIV-1 envelope glycoprotein trimer.
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21117239 A.Emileh, and C.F.Abrams (2011).
A mechanism by which binding of the broadly neutralizing antibody b12 unfolds the inner domain α1 helix in an engineered HIV-1 gp120.
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21288305 A.Schön, N.Madani, A.B.Smith, J.M.Lalonde, and E.Freire (2011).
Some binding-related drug properties are dependent on thermodynamic signature.
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21206085 B.Hong, X.T.Song, L.Rollins, L.Berry, X.F.Huang, and S.Y.Chen (2011).
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21468932 B.Wei, N.Han, H.Z.Liu, A.Rayner, and S.Rayner (2011).
Use of mutual information arrays to predict coevolving sites in the full length HIV gp120 protein for subtypes B and C.
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21357743 C.R.Ruprecht, A.Krarup, L.Reynell, A.M.Mann, O.F.Brandenberg, L.Berlinger, I.A.Abela, R.R.Regoes, H.F.Günthard, P.Rusert, and A.Trkola (2011).
MPER-specific antibodies induce gp120 shedding and irreversibly neutralize HIV-1.
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21479208 F.Breden, C.Lepik, N.S.Longo, M.Montero, P.E.Lipsky, and J.K.Scott (2011).
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21383973 F.Nawaz, C.Cicala, D.Van Ryk, K.E.Block, K.Jelicic, J.P.McNally, O.Ogundare, M.Pascuccio, N.Patel, D.Wei, A.S.Fauci, and J.Arthos (2011).
The genotype of early-transmitting HIV gp120s promotes α₄β₇-reactivity, revealing α₄β₇CD4+ T cells as key targets in mucosal transmission.
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21253014 F.Wegmann, G.Krashias, K.Lühn, K.Laamanen, S.Vieira, S.A.Jeffs, R.J.Shattock, and Q.J.Sattentau (2011).
A novel strategy for inducing enhanced mucosal HIV-1 antibody responses in an anti-inflammatory environment.
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21283793 H.Barroso, P.Borrego, I.Bártolo, J.M.Marcelino, C.Família, A.Quintas, and N.Taveira (2011).
Evolutionary and structural features of the C2, V3 and C3 envelope regions underlying the differences in HIV-1 and HIV-2 biology and infection.
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22113616 J.S.McLellan, M.Pancera, C.Carrico, J.Gorman, J.P.Julien, R.Khayat, R.Louder, R.Pejchal, M.Sastry, K.Dai, S.O'Dell, N.Patel, S.Shahzad-ul-Hussan, Y.Yang, B.Zhang, T.Zhou, J.Zhu, J.C.Boyington, G.Y.Chuang, D.Diwanji, I.Georgiev, Y.D.Kwon, D.Lee, M.K.Louder, S.Moquin, S.D.Schmidt, Z.Y.Yang, M.Bonsignori, J.A.Crump, S.H.Kapiga, N.E.Sam, B.F.Haynes, D.R.Burton, W.C.Koff, L.M.Walker, S.Phogat, R.Wyatt, J.Orwenyo, L.X.Wang, J.Arthos, C.A.Bewley, J.R.Mascola, G.J.Nabel, W.R.Schief, A.B.Ward, I.A.Wilson, and P.D.Kwong (2011).
Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9.
  Nature, 480, 336-343.
PDB codes: 3tcl 3u1s 3u2s 3u36 3u46 3u4b 3u4e
  21465559 L.T.Da, J.M.Quan, and Y.D.Wu (2011).
Understanding the binding mode and function of BMS-488043 against HIV-1 viral entry.
  Proteins, 79, 1810-1819.  
21377881 M.Caffrey (2011).
HIV envelope: challenges and opportunities for development of entry inhibitors.
  Trends Microbiol, 19, 191-197.  
22002224 M.Kim, Z.Y.Sun, K.D.Rand, X.Shi, L.Song, Y.Cheng, A.F.Fahmy, S.Majumdar, G.Ofek, Y.Yang, P.D.Kwong, J.H.Wang, J.R.Engen, G.Wagner, and E.L.Reinherz (2011).
Antibody mechanics on a membrane-bound HIV segment essential for GP41-targeted viral neutralization.
  Nat Struct Mol Biol, 18, 1235-1243.  
22139037 S.Moir, A.Malaspina, and A.S.Fauci (2011).
Prospects for an HIV vaccine: leading B cells down the right path.
  Nat Struct Mol Biol, 18, 1317-1321.  
20227370 A.Finzi, S.H.Xiang, B.Pacheco, L.Wang, J.Haight, A.Kassa, B.Danek, M.Pancera, P.D.Kwong, and J.Sodroski (2010).
Topological layers in the HIV-1 gp120 inner domain regulate gp41 interaction and CD4-triggered conformational transitions.
  Mol Cell, 37, 656-667.  
20463957 A.Hinz, D.Lutje Hulsik, A.Forsman, W.W.Koh, H.Belrhali, A.Gorlani, H.de Haard, R.A.Weiss, T.Verrips, and W.Weissenhorn (2010).
Crystal structure of the neutralizing Llama V(HH) D7 and its mode of HIV-1 gp120 interaction.
  PLoS One, 5, e10482.
PDB code: 2xa3
20232097 A.Malik, A.Firoz, V.Jha, E.Sunderasan, and S.Ahmad (2010).
Modeling the three-dimensional structures of an unbound single-chain variable fragment (scFv) and its hypothetical complex with a Corynespora cassiicola toxin, cassiicolin.
  J Mol Model, 16, 1883-1893.  
19922969 A.Nandi, C.L.Lavine, P.Wang, I.Lipchina, P.A.Goepfert, G.M.Shaw, G.D.Tomaras, D.C.Montefiori, B.F.Haynes, P.Easterbrook, J.E.Robinson, J.G.Sodroski, and X.Yang (2010).
Epitopes for broad and potent neutralizing antibody responses during chronic infection with human immunodeficiency virus type 1.
  Virology, 396, 339-348.  
20826338 B.E.Correia, Y.E.Ban, M.A.Holmes, H.Xu, K.Ellingson, Z.Kraft, C.Carrico, E.Boni, D.N.Sather, C.Zenobia, K.Y.Burke, T.Bradley-Hewitt, J.F.Bruhn-Johannsen, O.Kalyuzhniy, D.Baker, R.K.Strong, L.Stamatatos, and W.R.Schief (2010).
Computational design of epitope-scaffolds allows induction of antibodies specific for a poorly immunogenic HIV vaccine epitope.
  Structure, 18, 1116-1126.
PDB codes: 3lef 3lf6 3lf9 3lg7 3lh2 3lhp
19939935 B.Yu, D.P.Fonseca, S.M.O'Rourke, and P.W.Berman (2010).
Protease cleavage sites in HIV-1 gp120 recognized by antigen processing enzymes are conserved and located at receptor binding sites.
  J Virol, 84, 1513-1526.  
20194785 C.F.Abrams, and E.Vanden-Eijnden (2010).
Large-scale conformational sampling of proteins using temperature-accelerated molecular dynamics.
  Proc Natl Acad Sci U S A, 107, 4961-4966.  
20059334 D.H.Barouch, and B.Korber (2010).
HIV-1 vaccine development after STEP.
  Annu Rev Med, 61, 153-167.  
20705840 D.R.Burton, and R.A.Weiss (2010).
AIDS/HIV. A boost for HIV vaccine design.
  Science, 329, 770-773.  
19829304 D.S.Nikolic, and V.Piguet (2010).
Vaccines and microbicides preventing HIV-1, HSV-2, and HPV mucosal transmission.
  J Invest Dermatol, 130, 352-361.  
20053822 E.M.Bunnik, M.J.van Gils, M.S.Lobbrecht, L.Pisas, N.M.Nanlohy, D.van Baarle, A.C.van Nuenen, A.J.Hessell, and H.Schuitemaker (2010).
Emergence of monoclonal antibody b12-resistant human immunodeficiency virus type 1 variants during natural infection in the absence of humoral or cellular immune pressure.
  J Gen Virol, 91, 1354-1364.  
20376006 G.F.Schröder, M.Levitt, and A.T.Brunger (2010).
Super-resolution biomolecular crystallography with low-resolution data.
  Nature, 464, 1218-1222.  
20042512 G.Ofek, K.McKee, Y.Yang, Z.Y.Yang, J.Skinner, F.J.Guenaga, R.Wyatt, M.B.Zwick, G.J.Nabel, J.R.Mascola, and P.D.Kwong (2010).
Relationship between antibody 2F5 neutralization of HIV-1 and hydrophobicity of its heavy chain third complementarity-determining region.
  J Virol, 84, 2955-2962.  
20441761 G.Scarabelli, G.Morra, and G.Colombo (2010).
Predicting interaction sites from the energetics of isolated proteins: a new approach to epitope mapping.
  Biophys J, 98, 1966-1975.  
20052405 H.C.Kelker, V.R.Itri, and F.T.Valentine (2010).
A strategy for eliciting antibodies against cryptic, conserved, conformationally dependent epitopes of HIV envelope glycoprotein.
  PLoS One, 5, e8555.  
19955308 I.Douagi, M.N.Forsell, C.Sundling, S.O'Dell, Y.Feng, P.Dosenovic, Y.Li, R.Seder, K.Loré, J.R.Mascola, R.T.Wyatt, and G.B.Karlsson Hedestam (2010).
Influence of novel CD4 binding-defective HIV-1 envelope glycoprotein immunogens on neutralizing antibody and T-cell responses in nonhuman primates.
  J Virol, 84, 1683-1695.  
20718047 I.Shrivastava, and J.M.LaLonde (2010).
Fluctuation dynamics analysis of gp120 envelope protein reveals a topologically based communication network.
  Proteins, 78, 2935-2949.  
19824826 J.A.Hoxie (2010).
Toward an antibody-based HIV-1 vaccine.
  Annu Rev Med, 61, 135-152.  
20888479 J.Liu, E.R.Wright, and H.Winkler (2010).
3D visualization of HIV virions by cryoelectron tomography.
  Methods Enzymol, 483, 267-290.  
20335257 J.M.Binley, Y.E.Ban, E.T.Crooks, D.Eggink, K.Osawa, W.R.Schief, and R.W.Sanders (2010).
Role of complex carbohydrates in human immunodeficiency virus type 1 infection and resistance to antibody neutralization.
  J Virol, 84, 5637-5655.  
20147404 J.P.Julien, N.Huarte, R.Maeso, S.G.Taneva, A.Cunningham, J.L.Nieva, and E.F.Pai (2010).
Ablation of the complementarity-determining region H3 apex of the anti-HIV-1 broadly neutralizing antibody 2F5 abrogates neutralizing capacity without affecting core epitope binding.
  J Virol, 84, 4136-4147.  
20679402 J.Pietzsch, J.F.Scheid, H.Mouquet, F.Klein, M.S.Seaman, M.Jankovic, D.Corti, A.Lanzavecchia, and M.C.Nussenzweig (2010).
Human anti-HIV-neutralizing antibodies frequently target a conserved epitope essential for viral fitness.
  J Exp Med, 207, 1995-2002.  
20192810 J.R.Mascola, and D.C.Montefiori (2010).
The role of antibodies in HIV vaccines.
  Annu Rev Immunol, 28, 413-444.  
20523901 J.S.Klein, and P.J.Bjorkman (2010).
Few and far between: how HIV may be evading antibody avidity.
  PLoS Pathog, 6, e1000908.  
  20981030 K.H.Huang, D.Bonsall, A.Katzourakis, E.C.Thomson, S.J.Fidler, J.Main, D.Muir, J.N.Weber, A.J.Frater, R.E.Phillips, O.G.Pybus, P.J.Goulder, M.O.McClure, G.S.Cooke, and P.Klenerman (2010).
B-cell depletion reveals a role for antibodies in the control of chronic HIV-1 infection.
  Nat Commun, 1, 102.  
20702629 K.J.Doores, Z.Fulton, M.Huber, I.A.Wilson, and D.R.Burton (2010).
Antibody 2G12 recognizes di-mannose equivalently in domain- and nondomain-exchanged forms but only binds the HIV-1 glycan shield if domain exchanged.
  J Virol, 84, 10690-10699.
PDB code: 3oau
20852065 K.J.Doores, Z.Fulton, V.Hong, M.K.Patel, C.N.Scanlan, M.R.Wormald, M.G.Finn, D.R.Burton, I.A.Wilson, and B.G.Davis (2010).
A nonself sugar mimic of the HIV glycan shield shows enhanced antigenicity.
  Proc Natl Acad Sci U S A, 107, 17107-17112.
PDB codes: 3oay 3oaz 3ob0
  21267356 L.J.Gamble, and Q.L.Matthews (2010).
Current progress in the development of a prophylactic vaccine for HIV-1.
  Drug Des Devel Ther, 5, 9.  
20660185 L.Kong, C.C.Huang, S.J.Coales, K.S.Molnar, J.Skinner, Y.Hamuro, and P.D.Kwong (2010).
Local conformational stability of HIV-1 gp120 in unliganded and CD4-bound states as defined by amide hydrogen/deuterium exchange.
  J Virol, 84, 10311-10321.  
20299194 L.M.Walker, and D.R.Burton (2010).
Rational antibody-based HIV-1 vaccine design: current approaches and future directions.
  Curr Opin Immunol, 22, 358-366.  
20018688 L.Verkoczy, M.Diaz, T.M.Holl, Y.B.Ouyang, H.Bouton-Verville, S.M.Alam, H.X.Liao, G.Kelsoe, and B.F.Haynes (2010).
Autoreactivity in an HIV-1 broadly reactive neutralizing antibody variable region heavy chain induces immunologic tolerance.
  Proc Natl Acad Sci U S A, 107, 181-186.  
20845361 M.Hertje, M.Zhou, and U.Dietrich (2010).
Inhibition of HIV-1 entry: multiple keys to close the door.
  ChemMedChem, 5, 1825-1835.  
20610714 M.J.Duenas-Decamp, and P.R.Clapham (2010).
HIV-1 gp120 determinants proximal to the CD4 binding site shift protective glycans that are targeted by monoclonal antibody 2G12.
  J Virol, 84, 9608-9612.  
20210752 M.L.Bellows, and C.A.Floudas (2010).
Computational methods for de novo protein design and its applications to the human immunodeficiency virus 1, purine nucleoside phosphorylase, ubiquitin specific protease 7, and histone demethylases.
  Curr Drug Targets, 11, 264-278.  
20538861 M.Pancera, J.S.McLellan, X.Wu, J.Zhu, A.Changela, S.D.Schmidt, Y.Yang, T.Zhou, S.Phogat, J.R.Mascola, and P.D.Kwong (2010).
Crystal structure of PG16 and chimeric dissection with somatically related PG9: structure-function analysis of two quaternary-specific antibodies that effectively neutralize HIV-1.
  J Virol, 84, 8098-8110.
PDB codes: 3lrs 3mme
20080564 M.Pancera, S.Majeed, Y.E.Ban, L.Chen, C.C.Huang, L.Kong, Y.D.Kwon, J.Stuckey, T.Zhou, J.E.Robinson, W.R.Schief, J.Sodroski, R.Wyatt, and P.D.Kwong (2010).
Structure of HIV-1 gp120 with gp41-interactive region reveals layered envelope architecture and basis of conformational mobility.
  Proc Natl Acad Sci U S A, 107, 1166-1171.
PDB codes: 3jwd 3jwo
20439465 M.Raska, K.Takahashi, L.Czernekova, K.Zachova, S.Hall, Z.Moldoveanu, M.C.Elliott, L.Wilson, R.Brown, D.Jancova, S.Barnes, J.Vrbkova, M.Tomana, P.D.Smith, J.Mestecky, M.B.Renfrow, and J.Novak (2010).
Glycosylation patterns of HIV-1 gp120 depend on the type of expressing cells and affect antibody recognition.
  J Biol Chem, 285, 20860-20869.  
  20923574 M.Wen, R.Arora, H.Wang, L.Liu, J.T.Kimata, and P.Zhou (2010).
GPI-anchored single chain Fv--an effective way to capture transiently-exposed neutralization epitopes on HIV-1 envelope spike.
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20164234 P.Utachee, S.Nakamura, P.Isarangkura-Na-Ayuthaya, K.Tokunaga, P.Sawanpanyalert, K.Ikuta, W.Auwanit, and M.Kameoka (2010).
Two N-linked glycosylation sites in the V2 and C2 regions of human immunodeficiency virus type 1 CRF01_AE envelope glycoprotein gp120 regulate viral neutralization susceptibility to the human monoclonal antibody specific for the CD4 binding domain.
  J Virol, 84, 4311-4320.  
  20168075 P.W.Hammond (2010).
Accessing the human repertoire for broadly neutralizing HIV antibodies.
  MAbs, 2, 157-164.  
20463081 P.Wang, and X.Yang (2010).
Neutralization efficiency is greatly enhanced by bivalent binding of an antibody to epitopes in the V4 region and the membrane-proximal external region within one trimer of human immunodeficiency virus type 1 glycoproteins.
  J Virol, 84, 7114-7123.  
  21173880 Q.J.Sattentau, and A.J.McMichael (2010).
New templates for HIV-1 antibody-based vaccine design.
  F1000 Biol Rep, 2, 60.  
20357769 R.Diskin, P.M.Marcovecchio, and P.J.Bjorkman (2010).
Structure of a clade C HIV-1 gp120 bound to CD4 and CD4-induced antibody reveals anti-CD4 polyreactivity.
  Nat Struct Mol Biol, 17, 608-613.
PDB codes: 3lmj 3lqa
20534513 R.Pejchal, L.M.Walker, R.L.Stanfield, S.K.Phogat, W.C.Koff, P.Poignard, D.R.Burton, and I.A.Wilson (2010).
Structure and function of broadly reactive antibody PG16 reveal an H3 subdomain that mediates potent neutralization of HIV-1.
  Proc Natl Acad Sci U S A, 107, 11483-11488.
PDB codes: 3mug 3muh
  20860805 R.Ringe, M.Thakar, and J.Bhattacharya (2010).
Variations in autologous neutralization and CD4 dependence of b12 resistant HIV-1 clade C env clones obtained at different time points from antiretroviral naïve Indian patients with recent infection.
  Retrovirology, 7, 76.  
20949103 S.Gnanakaran, M.G.Daniels, T.Bhattacharya, A.S.Lapedes, A.Sethi, M.Li, H.Tang, K.Greene, H.Gao, B.F.Haynes, M.S.Cohen, G.M.Shaw, M.S.Seaman, A.Kumar, F.Gao, D.C.Montefiori, and B.Korber (2010).
Genetic signatures in the envelope glycoproteins of HIV-1 that associate with broadly neutralizing antibodies.
  PLoS Comput Biol, 6, e1000955.  
20089638 S.H.Xiang, A.Finzi, B.Pacheco, K.Alexander, W.Yuan, C.Rizzuto, C.C.Huang, P.D.Kwong, and J.Sodroski (2010).
A V3 loop-dependent gp120 element disrupted by CD4 binding stabilizes the human immunodeficiency virus envelope glycoprotein trimer.
  J Virol, 84, 3147-3161.  
20518719 S.Hearty, P.J.Conroy, B.V.Ayyar, B.Byrne, and R.O'Kennedy (2010).
Surface plasmon resonance for vaccine design and efficacy studies: recent applications and future trends.
  Expert Rev Vaccines, 9, 645-664.  
20822346 S.Paul, S.Planque, Y.Nishiyama, M.Escobar, and C.Hanson (2010).
Back to the future: covalent epitope-based HIV vaccine development.
  Expert Rev Vaccines, 9, 1027-1043.  
20186035 S.Planque, M.Salas, Y.Mitsuda, M.Sienczyk, M.A.Escobar, J.P.Mooney, M.K.Morris, Y.Nishiyama, D.Ghosh, A.Kumar, F.Gao, C.V.Hanson, and S.Paul (2010).
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PDB codes: 3go1 3mlr 3mls 3mlt 3mlu 3mlv 3mlw 3mlx 3mly 3mlz
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Resveratrol: its biologic targets and functional activity.
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PDB codes: 2eh7 2eh8
17721546 Y.Li, S.A.Migueles, B.Welcher, K.Svehla, A.Phogat, M.K.Louder, X.Wu, G.M.Shaw, M.Connors, R.T.Wyatt, and J.R.Mascola (2007).
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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.