Crystal Structure of the Herpesvirus Nuclear Egress Complex Provides Insights into Inner Nuclear Membrane Remodeling.

@article{ZeevBenMordehai2015CrystalSO,
  title={Crystal Structure of the Herpesvirus Nuclear Egress Complex Provides Insights into Inner Nuclear Membrane Remodeling.},
  author={Tzviya Zeev-Ben-Mordehai and Marion Weberruss and Michael Lorenz and Juliana Cheleski and Teresa Hellberg and Cathy Whittle and Kamel El Omari and Daven Vasishtan and Kyle Clayton Dent and Karl Harlos and Kati Franzke and Christoph Graf Vom Hagen and Barbara G. Klupp and Wolfram Antonin and Thomas C Mettenleiter and Kay Gr{\"u}newald},
  journal={Cell reports},
  year={2015},
  volume={13 12},
  pages={
          2645-52
        }
}
Although nucleo-cytoplasmic transport is typically mediated through nuclear pore complexes, herpesvirus capsids exit the nucleus via a unique vesicular pathway. Together, the conserved herpesvirus proteins pUL31 and pUL34 form the heterodimeric nuclear egress complex (NEC), which, in turn, mediates the formation of tight-fitting membrane vesicles around capsids at the inner nuclear membrane. Here, we present the crystal structure of the pseudorabies virus NEC. The structure revealed that a zinc… CONTINUE READING
BETA

Citations

Publications citing this paper.
SHOWING 1-10 OF 14 CITATIONS

References

Publications referenced by this paper.
SHOWING 1-10 OF 24 REFERENCES

Functional characterization of nuclear trafficking signals in pseudorabies virus pUL31

  • L. Paßvogel, B. G. Klupp, H. Granzow, W. Fuchs, T. C. Mettenleiter
  • J. Virol. 89, –2012. Reynolds, A.E., Ryckman, B.J…
  • 2015
1 Excerpt

Relationship between the architecture of zinc coordination and zinc binding affinity in proteins–insights into zinc regulation

  • A. zel
  • Metallomics
  • 2015

Similar Papers

Loading similar papers…