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Complex(antibody/HIV-1 fragment) PDB id
1acy
Jmol
Contents
Protein chains
215 a.a. *
221 a.a. *
Ligands
HIS-ILE-GLY-PRO-
GLY-ARG-ALA-PHE-
TYR-THR
* Residue conservation analysis
PDB id:
1acy
Name: Complex(antibody/HIV-1 fragment)
Title: Crystal structure of the principal neutralizing site of HIV- 1
Structure: Igg1-kappa 59.1 fab (light chain). Chain: l. Engineered: yes. Igg1-kappa 59.1 fab (heavy chain). Chain: h. Engineered: yes. HIV-1 gp120 (mn isolate). Chain: p. Fragment: fragment (residues 308 - 332).
Source: Mus musculus. House mouse. Organism_taxid: 10090. HIV-1 m:b_mn. Organism_taxid: 11696
Biol. unit: Dimer (from PQS)
Resolution:
3.00Å     R-factor:   0.210    
Authors: J.B.Ghiara,I.A.Wilson
Key ref: J.B.Ghiara et al. (1994). Crystal structure of the principal neutralization site of HIV-1. Science, 264, 82-85. PubMed id: 7511253 DOI: 10.1126/science.7511253
Date:
10-Feb-94     Release date:   31-Jul-94    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q66JS7  (Q66JS7_MOUSE) -  Igk protein
Seq:
Struc:
238 a.a.
215 a.a.*
Protein chain
Pfam   ArchSchema ?
P01869  (IGH1M_MOUSE) -  Ig gamma-1 chain C region, membrane-bound form
Seq:
Struc:
393 a.a.
221 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 27 residue positions (black crosses)

 

 
DOI no: 10.1126/science.7511253 Science 264:82-85 (1994)
PubMed id: 7511253  
 
 
Crystal structure of the principal neutralization site of HIV-1.
J.B.Ghiara, E.A.Stura, R.L.Stanfield, A.T.Profy, I.A.Wilson.
 
  ABSTRACT  
 
The crystal structure of a complex between a 24-amino acid peptide from the third variable (V3) loop of human immunodeficiency virus-type 1 (HIV-1) gp 120 and the Fab fragment of a broadly neutralizing antibody (59.1) was determined to 3 angstrom resolution. The tip of the V3 loop containing the Gly-Pro-Gly-Arg-Ala-Phe sequence adopts a double-turn conformation, which may be the basis of its conservation in many HIV-1 isolates. A complete map of the HIV-1 principal neutralizing determinant was constructed by stitching together structures of V3 loop peptides bound to 59.1 and to an isolate-specific (MN) neutralizing antibody (50.1). Structural conservation of the overlapping epitopes suggests that this biologically relevant conformation could be of use in the design of synthetic vaccines and drugs to inhibit HIV-1 entry and virus-related cellular fusion.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
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Differences in the mannose oligomer specificities of the closely related lectins from Galanthus nivalis and Zea mays strongly determine their eventual anti-HIV activity.
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21053260 M.Gupta, and V.S.Chauhan (2011).
De novo design of α,β-didehydrophenylalanine containing peptides: From models to applications.
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19281264 A.Mor, E.Segal, B.Mester, B.Arshava, O.Rosen, F.X.Ding, J.Russo, A.Dafni, F.Schvartzman, T.Scherf, F.Naider, and J.Anglister (2009).
Mimicking the structure of the V3 epitope bound to HIV-1 neutralizing antibodies.
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19117029 P.A.Galanakis, N.G.Kandias, A.K.Rizos, D.Morikis, E.Krambovitis, and G.A.Spyroulias (2009).
NMR evidence of charge-dependent interaction between various PND V3 and CCR5 N-terminal peptides.
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18566514 A.K.Dhillon, R.L.Stanfield, M.K.Gorny, C.Williams, S.Zolla-Pazner, and I.A.Wilson (2008).
Structure determination of an anti-HIV-1 Fab 447-52D-peptide complex from an epitaxially twinned data set.
  Acta Crystallogr D Biol Crystallogr, 64, 792-802.
PDB code: 3c2a
18068724 C.H.Bell, R.Pantophlet, A.Schiefner, L.A.Cavacini, R.L.Stanfield, D.R.Burton, and I.A.Wilson (2008).
Structure of antibody F425-B4e8 in complex with a V3 peptide reveals a new binding mode for HIV-1 neutralization.
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PDB code: 2qsc
16978155 A.M.Andrianov, and V.G.Veresov (2006).
Determination of structurally conservative amino acids of the HIV-1 protein gp120 V3 loop as promising targets for drug design by protein engineering approaches.
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16411186 P.Mathur, U.A.Ramagopal, S.Ramakumar, N.R.Jagannathan, and V.S.Chauhan (2006).
Stabilization of unusual structures in peptides using alpha,beta-dehydrophenylalanine: crystal and solution structures of Boc-Pro-DeltaPhe-Val-DeltaPhe-Ala-OMe and Boc-Pro-DeltaPhe-Gly-DeltaPhe-Ala-OMe.
  Biopolymers, 84, 298-309.  
16731948 R.L.Stanfield, M.K.Gorny, S.Zolla-Pazner, and I.A.Wilson (2006).
Crystal structures of human immunodeficiency virus type 1 (HIV-1) neutralizing antibody 2219 in complex with three different V3 peptides reveal a new binding mode for HIV-1 cross-reactivity.
  J Virol, 80, 6093-6105.
PDB codes: 2b0s 2b1a 2b1h
16361230 T.Watabe, H.Kishino, Y.Okuhara, and Y.Kitazoe (2006).
Fold recognition of the human immunodeficiency virus type 1 V3 loop and flexibility of its crown structure during the course of adaptation to a host.
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Vaccination of rhesus macaques with recombinant Mycobacterium bovis bacillus Calmette-Guérin Env V3 elicits neutralizing antibody-mediated protection against simian-human immunodeficiency virus with a homologous but not a heterologous V3 motif.
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15725757 O.Hartley, P.J.Klasse, Q.J.Sattentau, and J.P.Moore (2005).
V3: HIV's switch-hitter.
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PDB code: 1yt6
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The HF-SCF energy of HIV-1 MNgp120 V3 hairpin loop conformers.
  J Mol Model, 10, 367-372.  
14962377 P.D.Kwong (2004).
The 447-52D antibody: hitting HIV-1 where its armor is thickest.
  Structure, 12, 173-174.  
15386623 P.J.Cachia, D.J.Kao, and R.S.Hodges (2004).
Synthetic peptide vaccine development: measurement of polyclonal antibody affinity and cross-reactivity using a new peptide capture and release system for surface plasmon resonance spectroscopy.
  J Mol Recognit, 17, 540-557.  
14962380 R.L.Stanfield, M.K.Gorny, C.Williams, S.Zolla-Pazner, and I.A.Wilson (2004).
Structural rationale for the broad neutralization of HIV-1 by human monoclonal antibody 447-52D.
  Structure, 12, 193-204.
PDB code: 1q1j
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Genetic and phenotypic analyses of human immunodeficiency virus type 1 escape from a small-molecule CCR5 inhibitor.
  J Virol, 78, 2790-2807.  
15103622 S.T.Hsu, and A.M.Bonvin (2004).
Atomic insight into the CD4 binding-induced conformational changes in HIV-1 gp120.
  Proteins, 55, 582-593.  
12767116 P.J.Cachia, and R.S.Hodges (2003).
Synthetic peptide vaccine and antibody therapeutic development: prevention and treatment of Pseudomonas aeruginosa.
  Biopolymers, 71, 141-168.  
12719582 R.Pantophlet, I.A.Wilson, and D.R.Burton (2003).
Hyperglycosylated mutants of human immunodeficiency virus (HIV) type 1 monomeric gp120 as novel antigens for HIV vaccine design.
  J Virol, 77, 5889-5901.  
  12121655 J.Ding, A.D.Smith, S.C.Geisler, X.Ma, G.F.Arnold, and E.Arnold (2002).
Crystal structure of a human rhinovirus that displays part of the HIV-1 V3 loop and induces neutralizing antibodies against HIV-1.
  Structure, 10, 999.
PDB code: 1k5m
12186887 M.K.Gorny, C.Williams, B.Volsky, K.Revesz, S.Cohen, V.R.Polonis, W.J.Honnen, S.C.Kayman, C.Krachmarov, A.Pinter, and S.Zolla-Pazner (2002).
Human monoclonal antibodies specific for conformation-sensitive epitopes of V3 neutralize human immunodeficiency virus type 1 primary isolates from various clades.
  J Virol, 76, 9035-9045.  
12368322 S.Basmaciogullari, G.J.Babcock, D.Van Ryk, W.Wojtowicz, and J.Sodroski (2002).
Identification of conserved and variable structures in the human immunodeficiency virus gp120 glycoprotein of importance for CXCR4 binding.
  J Virol, 76, 10791-10800.  
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Assembly of a polytopic membrane protein structure from the solution structures of overlapping peptide fragments of bacteriorhodopsin.
  Biophys J, 81, 1029-1036.
PDB code: 1l0m
11369853 M.Monette, S.J.Opella, J.Greenwood, A.E.Willis, and R.N.Perham (2001).
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Conformational model for the consensus V3 loop of the envelope protein gp120 of HIV-1 in a 20% trifluoroethanol/water solution.
  Eur J Biochem, 268, 2620-2628.  
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Interaction of a bacterially expressed peptide from the receptor binding domain of Pseudomonas aeruginosa pili strain PAK with a cross-reactive antibody: conformation of the bound peptide.
  Biochemistry, 39, 14847-14864.  
10651813 A.Zvi, V.Tugarinov, G.A.Faiman, A.Horovitz, and J.Anglister (2000).
A model of a gp120 V3 peptide in complex with an HIV-neutralizing antibody based on NMR and mutant cycle-derived constraints.
  Eur J Biochem, 267, 767-779.  
11087390 E.Cabezas, M.Wang, P.W.Parren, R.L.Stanfield, and A.C.Satterthwait (2000).
A structure-based approach to a synthetic vaccine for HIV-1.
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10978173 J.G.Huisman, A.Carotenuto, A.F.Labrijn, C.H.Papavoine, J.D.Laman, M.M.Schellekens, M.H.Koppelman, and C.W.Hilbers (2000).
Recognition properties of V3-specific antibodies to V3 loop peptides derived from HIV-1 gp120 presented in multiple conformations.
  Biochemistry, 39, 10866-10876.  
10628815 J.Su, A.Palm, Y.Wu, S.Sandin, S.Höglund, and A.Vahlne (2000).
Deletion of the GPG motif in the HIV type 1 V3 loop does not abrogate infection in all cells.
  AIDS Res Hum Retroviruses, 16, 37-48.  
11009623 L.Kirnarsky, O.Prakash, S.M.Vogen, M.Nomoto, M.A.Hollingsworth, and S.Sherman (2000).
Structural effects of O-glycosylation on a 15-residue peptide from the mucin (MUC1) core protein.
  Biochemistry, 39, 12076-12082.  
10681015 N.T.Tran, M.Taverna, M.Chevalier, and D.Ferrier (2000).
One-step capillary isoelectric focusing for the separation of the recombinant human immunodeficiency virus envelope glycoprotein glycoforms.
  J Chromatogr A, 866, 121-135.  
11193052 P.B.Furtado, R.Furmonaviciene, J.McElveen, H.F.Sewell, and F.Shakib (2000).
Prediction of the interacting surfaces in a trimolecular complex formed between the major dust mite allergen Der p 1, a mouse monoclonal anti-Der p 1 antibody, and its anti-idiotype.
  Mol Pathol, 53, 324-332.  
  10801487 V.Tugarinov, A.Zvi, R.Levy, Y.Hayek, S.Matsushita, and J.Anglister (2000).
NMR structure of an anti-gp120 antibody complex with a V3 peptide reveals a surface important for co-receptor binding.
  Structure, 8, 385-395.
PDB code: 1qnz
10985765 X.Zhu, C.Borchers, R.J.Bienstock, and K.B.Tomer (2000).
Mass spectrometric characterization of the glycosylation pattern of HIV-gp120 expressed in CHO cells.
  Biochemistry, 39, 11194-11204.  
  10380013 A.Ota, A.N.Bautista, M.L.Yadav, and S.Ueda (1999).
Anti-P30-52 monoclonal antibody cross-reacted to Env V3 and inhibited the viral multiplication of HIV-1-infected MT-4 cells.
  Hybridoma, 18, 139-147.  
10223339 A.Zhang, S.C.Geisler, A.D.Smith, D.A.Resnick, M.L.Li, C.Y.Wang, D.J.Looney, F.Wong-Staal, E.Arnold, and G.F.Arnold (1999).
A disulfide-bound HIV-1 V3 loop sequence on the surface of human rhinovirus 14 induces neutralizing responses against HIV-1.
  Biol Chem, 380, 365-374.  
10451557 B.Selisko, A.F.Licea, B.Becerril, F.Zamudio, L.D.Possani, and E.Horjales (1999).
Antibody BCF2 against scorpion toxin Cn2 from Centuroides noxius Hoffmann: primary structure and three-dimensional model as free Fv fragment and complexed with its antigen.
  Proteins, 37, 130-143.  
10491120 E.S.Calderon-Aranda, B.Selisko, E.J.York, G.B.Gurrola, J.M.Stewart, and L.D.Possani (1999).
Mapping of an epitope recognized by a neutralizing monoclonal antibody specific to toxin Cn2 from the scorpion Centruroides noxius, using discontinuous synthetic peptides.
  Eur J Biochem, 264, 746-755.  
10221533 G.V.Quinnan, P.F.Zhang, D.W.Fu, M.Dong, and H.J.Alter (1999).
Expression and characterization of HIV type 1 envelope protein associated with a broadly reactive neutralizing antibody response.
  AIDS Res Hum Retroviruses, 15, 561-570.  
  9847381 H.M.Vu, D.Myers, R.de Lorimier, T.J.Matthews, M.A.Moody, C.Heinly, J.V.Torres, B.F.Haynes, and L.Spicer (1999).
Nuclear magnetic resonance analysis of solution conformations in C4-V3 hybrid peptides derived from human immunodeficiency virus (HIV) type 1 gp120: relation to specificity of peptide-induced anti-HIV neutralizing antibodies.
  J Virol, 73, 746-750.  
  10333243 K.Ichiyama, D.Ishikawa, Y.Tanaka, T.Kashiwa, Y.Koyanagi, S.Handa, A.Yamashita, M.Fukushi, N.Yamamoto, and T.Taki (1999).
Epitope mapping of rat neutralizing monoclonal antibody against human immunodeficiency virus type-1 by a phage peptide library: comparison with ELISA using synthetic peptides.
  Viral Immunol, 12, 57-66.  
  10368281 R.Stanfield, E.Cabezas, A.Satterthwait, E.Stura, A.Profy, and I.Wilson (1999).
Dual conformations for the HIV-1 gp120 V3 loop in complexes with different neutralizing fabs.
  Structure, 7, 131-142.
PDB codes: 1f58 2f58 3f58
  9420270 A.D.Smith, S.C.Geisler, A.A.Chen, D.A.Resnick, B.M.Roy, P.J.Lewi, E.Arnold, and G.F.Arnold (1998).
Human rhinovirus type 14:human immunodeficiency virus type 1 (HIV-1) V3 loop chimeras from a combinatorial library induce potent neutralizing antibody responses against HIV-1.
  J Virol, 72, 651-659.  
  9420273 J.C.Plantier, S.Le Pogam, F.Poisson, L.Buzelay, B.Lejeune, and F.Barin (1998).
Extent of antigenic diversity in the V3 region of the surface glycoprotein, gp120, of human immunodeficiency virus type 1 group M and consequences for serotyping.
  J Virol, 72, 677-683.  
  9696861 K.E.Follis, M.Trahey, R.A.LaCasse, and J.H.Nunberg (1998).
Continued utilization of CCR5 coreceptor by a newly derived T-cell line-adapted isolate of human immunodeficiency virus type 1.
  J Virol, 72, 7603-7608.  
9620614 M.A.Molins, M.A.Contreras, I.Fita, and M.Pons (1998).
Solution conformation of an immunogenic peptide from HRV2: comparison with the conformation found in a complex with a Fab fragment of an anti-HRV2 neutralizing antibody.
  J Pept Sci, 4, 101-110.  
9851371 M.Dettin, C.Scarinci, C.Zanotto, R.Roncon, A.De Rossi, and C.Di Bello (1998).
Biological and conformational studies on analogues of a synthetic peptide enhancing HIV-1 infection.
  J Pept Sci, 4, 436-448.  
9335536 A.P.Campbell, D.L.Bautista, B.Tripet, W.Y.Wong, R.T.Irvin, R.S.Hodges, and B.D.Sykes (1997).
Solution secondary structure of a bacterially expressed peptide from the receptor binding domain of Pseudomonas aeruginosa pili strain PAK: A heteronuclear multidimensional NMR study.
  Biochemistry, 36, 12791-12801.  
9214308 A.Zvi, D.J.Feigelson, Y.Hayek, and J.Anglister (1997).
Conformation of the principal neutralizing determinant of human immunodeficiency virus type 1 in complex with an anti-gp120 virus neutralizing antibody studied by two-dimensional nuclear magnetic resonance difference spectroscopy.
  Biochemistry, 36, 8619-8627.  
9130694 E.A.Hewat, N.Verdaguer, I.Fita, W.Blakemore, S.Brookes, A.King, J.Newman, E.Domingo, M.G.Mateu, and D.I.Stuart (1997).
Structure of the complex of an Fab fragment of a neutralizing antibody with foot-and-mouth disease virus: positioning of a highly mobile antigenic loop.
  EMBO J, 16, 1492-1500.
PDB code: 1qgc
  9100986 J.Cook, and B.H.Barber (1997).
Recombinant antibodies with conformationally constrained HIV type 1 epitope inserts elicit glycoprotein 160-specific antibody responses in vivo.
  AIDS Res Hum Retroviruses, 13, 449-460.  
  9371578 M.Schreiber, C.Wachsmuth, H.Müller, S.Odemuyiwa, H.Schmitz, S.Meyer, B.Meyer, and J.Schneider-Mergener (1997).
The V3-directed immune response in natural human immunodeficiency virus type 1 infection is predominantly directed against a variable, discontinuous epitope presented by the gp120 V3 domain.
  J Virol, 71, 9198-9205.  
9289017 P.L.Yeagle, J.L.Alderfer, and A.D.Albert (1997).
Three-dimensional structure of the cytoplasmic face of the G protein receptor rhodopsin.
  Biochemistry, 36, 9649-9654.  
9770649 P.Tsang, X.Mu, G.Wu, and P.J.Durda (1997).
NMR study and comparison of the antigenic properties of a peptide recognized by two HIV-1 neutralizing antibodies.
  J Mol Recognit, 10, 256-261.  
9312273 X.Huang, J.J.Barchi, F.D.Lung, P.P.Roller, P.L.Nara, J.Muschik, and R.R.Garrity (1997).
Glycosylation affects both the three-dimensional structure and antibody binding properties of the HIV-1IIIB GP120 peptide RP135.
  Biochemistry, 36, 10846-10856.  
9037041 Y.Yamaguchi, and T.Gojobori (1997).
Evolutionary mechanisms and population dynamics of the third variable envelope region of HIV within single hosts.
  Proc Natl Acad Sci U S A, 94, 1264-1269.  
8784355 A.Desmyter, T.R.Transue, M.A.Ghahroudi, M.H.Thi, F.Poortmans, R.Hamers, S.Muyldermans, and L.Wyns (1996).
Crystal structure of a camel single-domain VH antibody fragment in complex with lysozyme.
  Nat Struct Biol, 3, 803-811.
PDB code: 1mel
  8834457 D.Bhattacharyya, B.R.Brooks, and L.Callahan (1996).
Positioning of positively charged residues in the V3 loop correlates with HIV type 1 syncytium-inducing phenotype.
  AIDS Res Hum Retroviruses, 12, 83-90.  
8811340 G.Scarlatti, T.Leitner, V.Hodara, M.Jansson, A.Karlsson, J.Wahlberg, P.Rossi, M.Uhlén, E.M.Fenyö, and J.Albert (1996).
Interplay of HIV-1 phenotype and neutralizing antibody response in pathogenesis of AIDS.
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8611499 H.M.Vu, R.de Lorimier, M.A.Moody, B.F.Haynes, and L.D.Spicer (1996).
Conformational preferences of a chimeric peptide HIV-1 immunogen from the C4-V3 domains of gp120 envelope protein of HIV-1 CAN0A based on solution NMR: comparison to a related immunogenic peptide from HIV-1 RF.
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  8834458 I.J.Lauder, H.J.Lin, E.B.Siwak, and F.B.Hollinger (1996).
Kernel density analysis of variable and conserved regions of the envelope proteins of human immunodeficiency virus type 1 and associated epitopes.
  AIDS Res Hum Retroviruses, 12, 91-97.  
8639672 J.Cacia, R.Keck, L.G.Presta, and J.Frenz (1996).
Isomerization of an aspartic acid residue in the complementarity-determining regions of a recombinant antibody to human IgE: identification and effect on binding affinity.
  Biochemistry, 35, 1897-1903.  
8727315 J.E.Hansen, O.Lund, J.O.Nielsen, S.Brunak, and J.E.Hansen (1996).
Prediction of the secondary structure of HIV-1 gp120.
  Proteins, 25, 1.  
  8676469 M.A.Handley, R.T.Steigbigel, and S.A.Morrison (1996).
A role for urokinase-type plasminogen activator in human immunodeficiency virus type 1 infection of macrophages.
  J Virol, 70, 4451-4456.  
  8893048 P.J.Bickel, P.C.Cosman, R.A.Olshen, P.C.Spector, A.G.Rodrigo, and J.I.Mullins (1996).
Covariability of V3 loop amino acids.
  AIDS Res Hum Retroviruses, 12, 1401-1411.  
8620873 R.L.Markert, H.Ruppach, S.Gehring, U.Dietrich, D.F.Mierke, M.Köck, H.Rübsamen-Waigmann, and C.Griesinger (1996).
Secondary structural elements as a basis for antibody recognition in the immunodominant region of human immunodeficiency viruses 1 and 2.
  Eur J Biochem, 237, 188-204.  
8617252 W.F.Vranken, M.Budesinsky, J.C.Martins, F.Fant, K.Boulez, H.Gras-Masse, and F.A.Borremans (1996).
Conformational features of a synthetic cyclic peptide corresponding to the complete V3 loop of the RF HIV-1 strain in water and water/trifluoroethanol solutions.
  Eur J Biochem, 236, 100-108.  
8619951 A.R.Neurath, A.K.Debnath, N.Strick, Y.Y.Li, K.Lin, and S.Jiang (1995).
Blocking of CD4 cell receptors for the human immunodeficiency virus type 1 (HIV-1) by chemically modified bovine milk proteins: potential for AIDS prophylaxis.
  J Mol Recognit, 8, 304-316.  
9052975 A.R.Neurath, N.Strick, and A.K.Debnath (1995).
Structural requirements for and consequences of an antiviral porphyrin binding to the V3 loop of the human immunodeficiency virus (HIV-1) envelope glycoprotein gp120.
  J Mol Recognit, 8, 345-357.  
  7884887 D.A.Resnick, A.D.Smith, S.C.Gesiler, A.Zhang, E.Arnold, and G.F.Arnold (1995).
Chimeras from a human rhinovirus 14-human immunodeficiency virus type 1 (HIV-1) V3 loop seroprevalence library induce neutralizing responses against HIV-1.
  J Virol, 69, 2406-2411.  
  7576915 G.A.Pestano, K.S.Hosford, A.I.Spira, J.Riley, J.M.Xie, N.Sewankambo, L.Brown, D.D.Ho, and W.M.Boto (1995).
Seroreactivity of analogous antigenic epitopes in glycoprotein 120 expressed in HIV-1 subtypes A, B, C, and D.
  AIDS Res Hum Retroviruses, 11, 589-596.  
7816840 J.D.Fontenot, J.M.Gatewood, S.V.Mariappan, C.P.Pau, B.S.Parekh, J.R.George, and G.Gupta (1995).
Human immunodeficiency virus (HIV) antigens: structure and serology of multivalent human mucin MUC1-HIV V3 chimeric proteins.
  Proc Natl Acad Sci U S A, 92, 315-319.  
  8573370 J.P.Langedijk, G.Zwart, J.Goudsmit, and R.H.Meloen (1995).
Fine specificity of antibody recognition may predict amino acid substitution in the third variable region of gp120 during HIV type 1 infection.
  AIDS Res Hum Retroviruses, 11, 1153-1162.  
  7527082 J.P.Moore, A.Trkola, B.Korber, L.J.Boots, J.A.Kessler, F.E.McCutchan, J.Mascola, D.D.Ho, J.Robinson, and A.J.Conley (1995).
A human monoclonal antibody to a complex epitope in the V3 region of gp120 of human immunodeficiency virus type 1 has broad reactivity within and outside clade B.
  J Virol, 69, 122-130.  
7539711 M.W.Wien, D.J.Filman, E.A.Stura, S.Guillot, F.Delpeyroux, R.Crainic, and J.M.Hogle (1995).
Structure of the complex between the Fab fragment of a neutralizing antibody for type 1 poliovirus and its viral epitope.
  Nat Struct Biol, 2, 232-243.
PDB code: 1fpt
  7537661 N.Verdaguer, M.G.Mateu, D.Andreu, E.Giralt, E.Domingo, and I.Fita (1995).
Structure of the major antigenic loop of foot-and-mouth disease virus complexed with a neutralizing antibody: direct involvement of the Arg-Gly-Asp motif in the interaction.
  EMBO J, 14, 1690-1696.  
  7983725 N.Yahi, J.M.Sabatier, S.Baghdiguian, F.Gonzalez-Scarano, and J.Fantini (1995).
Synthetic multimeric peptides derived from the principal neutralization domain (V3 loop) of human immunodeficiency virus type 1 (HIV-1) gp120 bind to galactosylceramide and block HIV-1 infection in a human CD4-negative mucosal epithelial cell line.
  J Virol, 69, 320-325.  
7773739 R.L.Stanfield, and I.A.Wilson (1995).
Protein-peptide interactions.
  Curr Opin Struct Biol, 5, 103-113.  
  8573396 T.C.Vancott, V.R.Polonis, L.D.Loomis, N.L.Michael, P.L.Nara, and D.L.Birx (1995).
Differential role of V3-specific antibodies in neutralization assays involving primary and laboratory-adapted isolates of HIV type 1.
  AIDS Res Hum Retroviruses, 11, 1379-1391.  
  7742034 W.R.Gallaher, J.M.Ball, R.F.Garry, A.M.Martin-Amedee, and R.C.Montelaro (1995).
A general model for the surface glycoproteins of HIV and other retroviruses.
  AIDS Res Hum Retroviruses, 11, 191-202.  
7971973 D.F.Lake, S.F.Schluter, E.Wang, R.M.Bernstein, A.B.Edmundson, and J.J.Marchalonis (1994).
Autoantibodies to the alpha/beta T-cell receptors in human immunodeficiency virus infection: dysregulation and mimicry.
  Proc Natl Acad Sci U S A, 91, 10849-10853.  
7536111 I.A.Wilson, and R.L.Stanfield (1994).
Antibody-antigen interactions: new structures and new conformational changes.
  Curr Opin Struct Biol, 4, 857-867.  
  7966630 J.F.Morris, E.J.Sternberg, L.Gutshall, S.R.Petteway, and L.A.Ivanoff (1994).
Effect of a single amino acid substitution in the V3 domain of the human immunodeficiency virus type 1: generation of revertant viruses to overcome defects in infectivity in specific cell types.
  J Virol, 68, 8380-8385.  
7696460 J.N.Herron, A.H.Terry, S.Johnston, X.M.He, L.W.Guddat, E.W.Voss, and A.B.Edmundson (1994).
High resolution structures of the 4-4-20 Fab-fluorescein complex in two solvent systems: effects of solvent on structure and antigen-binding affinity.
  Biophys J, 67, 2167-2183.  
  7538846 K.Lim, J.X.Ho, K.Keeling, G.L.Gilliland, X.Ji, F.Rüker, and D.C.Carter (1994).
Three-dimensional structure of Schistosoma japonicum glutathione S-transferase fused with a six-amino acid conserved neutralizing epitope of gp41 from HIV.
  Protein Sci, 3, 2233-2244.
PDB code: 1gne
  7534097 K.Sherefa, M.Sällberg, and A.Sönnerborg (1994).
Evidence of no change in V3 loop antibody recognition pattern in HIV type 1-infected Ethiopians between 1988 and 1993.
  AIDS Res Hum Retroviruses, 10, 1551-1556.  
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.