Efficient Fusion at Neutral pH by Human Immunodeficiency Virus gp41 Trimers Containing the Fusion Peptide and Transmembrane Domains.

@article{Liang2018EfficientFA,
  title={Efficient Fusion at Neutral pH by Human Immunodeficiency Virus gp41 Trimers Containing the Fusion Peptide and Transmembrane Domains.},
  author={Sisheng Liang and Punsisi Upeka Ratnayake and Christopher M. Keinath and Lihui Jia and Rebecca J. Wolfe and Ahinsa Ranaweera and David P Weliky},
  journal={Biochemistry},
  year={2018},
  volume={57 7},
  pages={
          1219-1235
        }
}
Human immunodeficiency virus (HIV) is membrane-enveloped, and an initial infection step is joining/fusion of viral and cell membranes. This step is catalyzed by gp41, which is a single-pass integral viral membrane protein. The protein contains an ∼170-residue ectodomain located outside the virus that is important for fusion and includes the fusion peptide (FP), N-helix, loop, C-helix, and viral membrane-proximal external region (MPER). The virion initially has noncovalent complexes between… CONTINUE READING
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References

Publications referenced by this paper.
SHOWING 1-10 OF 39 REFERENCES

Insights into the conformation of the membrane

J. Roche
  • 2016

Structural basis for membrane anchoring of HIV-1 envelope spike

J. J. Chou
  • Science
  • 2016

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