HIV-1 Nef protein: Purification, crystallizations, and preliminary X- ray diffraction studies

P. Franken, S. Arold, A. Padilla, M. Bodeus, F. Hoh, M. P. Strub, M. Boyer, M. Jullien, R. Benarous, C. Dumas*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

23 Scopus citations


Human immunodeficiency virus Nef protein accelerates virulent progression of AIDS by its interaction with specific cellular proteins involved in cellular activation and signal transduction. Here we report the purification and crystallization of the conserved core of HIV-1(LAI) Nef protein in the unliganded form and in complex with the wild-type SH3 domain of the p59(fyn) protein-tyrosine kinase. One-dimensional NMR experiments show that full-length protein and truncated fragment corresponding to the product of HIV-1 protease cleavage have a well-folded compact tertiary structure. The ligand-free HIV-1 Nef(core) protein forms cubic crystals belonging to space group P23 with unit cell dimensions of a = b = c = 86.4 Å. The Nef-Fyn SH3 cocrystals belong to the space group P6122 or its enantiomorph, P6522, with unit cell dimensions of a = b = 108.2 Å and c = 223.7 Å. Both crystal forms diffract to a resolution limit of 3.0 Å resolution using synchrotron radiation, and are thus suitable for X-ray structure determination.

Original languageEnglish (US)
Pages (from-to)2681-2683
Number of pages3
JournalProtein Science
Issue number12
StatePublished - Dec 1997
Externally publishedYes


  • Crystallization
  • HIV-1
  • Nef
  • SH3 domain
  • Src kinase family

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


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