The extracellular domain of immunodeficiency virus gp41 protein: expression in Escherichia coli, purification, and crystallization

Protein Sci. 1997 Aug;6(8):1653-60. doi: 10.1002/pro.5560060806.


The env gene of SIV and HIV-1 encodes a single glycoprotein gp 160, which is processed to give a noncovalent complex of the soluble glycoprotein gp120 and the transmembrane glycoprotein gp41. The extracellular region (ectodomain), minus the N-terminal fusion peptide, of gp41 from HIV-1 (residues 27-154) and SIV (residues 27-149) have been expressed in Escherichia coli. These insoluble proteins were solubilized and subjected to a simple purification and folding scheme, which results in high yields of soluble protein. Purified proteins have a trimeric subunit composition and high alpha-helical content, consistent with the predicted coil-coil structure. SIV gp41 containing a double cysteine mutation was crystallized. The crystals are suitable for X-ray structure determination and, preliminary analysis, together with additional biochemical evidence, indicates that the gp41 trimer is arranged as a parallel bundle with threefold symmetry.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Chromatography, Gel
  • Cloning, Molecular
  • Crystallography, X-Ray
  • Electrophoresis, Polyacrylamide Gel
  • Escherichia coli / genetics
  • HIV Envelope Protein gp41 / chemistry
  • HIV Envelope Protein gp41 / genetics*
  • HIV Envelope Protein gp41 / isolation & purification
  • HIV-1 / chemistry*
  • Protein Conformation
  • Protein Folding


  • HIV Envelope Protein gp41