Molecular structure and biochemical properties of the HCCH-Zn2+ site in HIV-1 Vif.

@article{Giri2009MolecularSA,
  title={Molecular structure and biochemical properties of the HCCH-Zn2+ site in HIV-1 Vif.},
  author={Kalyan Giri and Robert Scott and Ernest L. Maynard},
  journal={Biochemistry},
  year={2009},
  volume={48 33},
  pages={7969-78}
}
Virion infectivity factor (Vif) is an HIV accessory protein that is essential for the infection of CD4(+) T cells. Vif recruits a Cullin 5 (Cul5)-based ubiquitin ligase that targets a host cytidine deaminase, apolipoprotein B mRNA editing enzyme catalytic polypeptide-like 3G (APOBEC3G), for proteasomal degradation. The Vif N-terminus binds APOBEC3G, and the C-terminus interacts with the Cul5-based ubiquitin ligase machinery. Within the C-terminus, a highly conserved H(108)-X(5)-C(114)-X(17-18… CONTINUE READING
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2009)Conformational analysis of apeptide approximating the HCCH motif in HIV-1 Vif

  • K. Giri, E. L. andMaynard
  • Peptide Sci. (in press)
  • 2009

Conformational analysis of apeptide approximating the HCCH motif in HIV - 1 Vif

  • K. Giri, E. L. andMaynard
  • Peptide Sci .
  • 2009

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