1CE4
CONFORMATIONAL MODEL FOR THE CONSENSUS V3 LOOP OF THE ENVELOPE PROTEIN GP120 OF HIV-1
Summary for 1CE4
| Entry DOI | 10.2210/pdb1ce4/pdb |
| Descriptor | PROTEIN (V3 LOOP OF HIV-1 ENVELOPE PROTEIN) (1 entity in total) |
| Functional Keywords | amphipathic helix, hiv infection, viral protein |
| Cellular location | Surface protein gp120: Virion membrane ; Peripheral membrane protein . Transmembrane protein gp41: Virion membrane ; Single-pass type I membrane protein : P20871 |
| Total number of polymer chains | 1 |
| Total formula weight | 3905.41 |
| Authors | Vranken, W.F.,Fant, F.,Budesinsky, M.,Borremans, F.A.M. (deposition date: 1999-03-15, release date: 1999-03-18, Last modification date: 2024-10-30) |
| Primary citation | Vranken, W.F.,Budesinsky, M.,Fant, F.,Boulez, K.,Borremans, F.A. The complete Consensus V3 loop peptide of the envelope protein gp120 of HIV-1 shows pronounced helical character in solution. FEBS Lett., 374:117-121, 1995 Cited by PubMed 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 JN 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. PubMed: 7589496DOI: 10.1016/0014-5793(95)01086-T PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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