1CE4

CONFORMATIONAL MODEL FOR THE CONSENSUS V3 LOOP OF THE ENVELOPE PROTEIN GP120 OF HIV-1

1CE4 の概要

• エントリーDOI: 10.2210/pdb1ce4/pdb
• 分子名称: PROTEIN (V3 LOOP OF HIV-1 ENVELOPE PROTEIN) (1 entity in total)
• 機能のキーワード: amphipathic helix, hiv infection, viral protein
• 細胞内の位置: Surface protein gp120: Virion membrane ; Peripheral membrane protein . Transmembrane protein gp41: Virion membrane ; Single-pass type I membrane protein : P20871
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3905.41

構造登録者

Vranken, W.F.,Fant, F.,Budesinsky, M.,Borremans, F.A.M. (登録日: 1999-03-15, 公開日: 1999-03-18, 最終更新日: 2024-10-30)

主引用文献

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

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: 7589496
DOI: 10.1016/0014-5793(95)01086-T

実験手法

SOLUTION NMR