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The complete consensus V3 loop peptide of the envelope protein gp120 of HIV-1 shows pronounced helical character in solution

(1995) FEBS LETTERS. 374(1). p.117-121
Author
Organization
Abstract
The disulfide bridge closed cyclic peptide corresponding to the whole Consensus V3 loop of the envelope protein gp120 of HIV-1 was examined by proton 2D-NMR spectroscopy in water and in a 20% trifluoroethanol/water solution. In water, NOE data support a beta-turn conformation for the central conservative GPGR region and point towards partial formation of a helix in the C-terminal part. Upon addition of trifluoroethanol, a C-terminal helix is formed. This is evidenced by NOE data, alpha-proton chemical shift changes and changes in the J(N alpha) vicinal coupling constants. The C-terminal helix is amphipathic and also occurs in other examined strains, It could therefore be an important feature for the functioning of the V3 loop.
Keywords
NMR, CONSENSUS SEQUENCE V3 LOOP, CONFORMATION IN SOLUTION, AMPHIPATHIC HELIX, GP120, HIV-1, IMMUNODEFICIENCY-VIRUS TYPE-1, PRINCIPAL NEUTRALIZING DETERMINANT, HUMAN MONOCLONAL-ANTIBODIES, CD4 BINDING-SITE, GLYCOPROTEIN GP120, SOLUBLE CD4, SEQUENCE, DOMAIN, CELLS, SPECTROSCOPY

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Chicago
Vranken, Wim, M Budesinsky, Franky Fant, Kris Boulez, and Frans Borremans. 1995. “The Complete Consensus V3 Loop Peptide of the Envelope Protein Gp120 of HIV-1 Shows Pronounced Helical Character in Solution.” Febs Letters 374 (1): 117–121.
APA
Vranken, W., Budesinsky, M., Fant, F., Boulez, K., & Borremans, F. (1995). The complete consensus V3 loop peptide of the envelope protein gp120 of HIV-1 shows pronounced helical character in solution. FEBS LETTERS, 374(1), 117–121.
Vancouver
1.
Vranken W, Budesinsky M, Fant F, Boulez K, Borremans F. The complete consensus V3 loop peptide of the envelope protein gp120 of HIV-1 shows pronounced helical character in solution. FEBS LETTERS. 1995;374(1):117–21.
MLA
Vranken, Wim, M Budesinsky, Franky Fant, et al. “The Complete Consensus V3 Loop Peptide of the Envelope Protein Gp120 of HIV-1 Shows Pronounced Helical Character in Solution.” FEBS LETTERS 374.1 (1995): 117–121. Print.
@article{195808,
  abstract     = {The disulfide bridge closed cyclic peptide corresponding to the whole Consensus V3 loop of the envelope protein gp120 of HIV-1 was examined by proton 2D-NMR spectroscopy in water and in a 20\% trifluoroethanol/water solution. In water, NOE data support a beta-turn conformation for the central conservative GPGR region and point towards partial formation of a helix in the C-terminal part. Upon addition of trifluoroethanol, a C-terminal helix is formed. This is evidenced by NOE data, alpha-proton chemical shift changes and changes in the J(N alpha) vicinal coupling constants. The C-terminal helix is amphipathic and also occurs in other examined strains, It could therefore be an important feature for the functioning of the V3 loop.},
  author       = {Vranken, Wim and Budesinsky, M and Fant, Franky and Boulez, Kris and Borremans, Frans},
  issn         = {0014-5793},
  journal      = {FEBS LETTERS},
  keyword      = {NMR,CONSENSUS SEQUENCE V3 LOOP,CONFORMATION IN SOLUTION,AMPHIPATHIC HELIX,GP120,HIV-1,IMMUNODEFICIENCY-VIRUS TYPE-1,PRINCIPAL NEUTRALIZING DETERMINANT,HUMAN MONOCLONAL-ANTIBODIES,CD4 BINDING-SITE,GLYCOPROTEIN GP120,SOLUBLE CD4,SEQUENCE,DOMAIN,CELLS,SPECTROSCOPY},
  language     = {eng},
  number       = {1},
  pages        = {117--121},
  title        = {The complete consensus V3 loop peptide of the envelope protein gp120 of HIV-1 shows pronounced helical character in solution},
  url          = {http://dx.doi.org/10.1016/0014-5793(95)01086-T},
  volume       = {374},
  year         = {1995},
}

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