Identification of a conserved domain of the HIV-1 transmembrane protein gp41 which interacts with cholesteryl groups.

@article{Vincent2002IdentificationOA,
  title={Identification of a conserved domain of the HIV-1 transmembrane protein gp41 which interacts with cholesteryl groups.},
  author={Nadine Vincent and Christian Genin and Etienne Malvoisin},
  journal={Biochimica et biophysica acta},
  year={2002},
  volume={1567 1-2},
  pages={157-64}
}
A soluble form of the HIV-1 envelope glycoprotein gp160 devoid of the transmembrane anchor domain was found to bind to cholesteryl-hemisuccinate agarose. The external subunit gp120 failed to bind to the resin, suggesting that the site responsible for the binding to cholesterol was located in the transmembrane protein gp41. We constructed a series of maltose binding protein (MBP) fusion proteins representing overlapping fragments of the gp41 molecule and we studied their capacity to bind to… CONTINUE READING
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