The carboxy-terminal domain initiates trimerization of bacteriophage T4 fibritin.

@article{Letarov1999TheCD,
  title={The carboxy-terminal domain initiates trimerization of bacteriophage T4 fibritin.},
  author={Andrei V Letarov and Yuri Y. Londer and Sergei P. Boudko and Vadim V. Mesyanzhinov},
  journal={Biochemistry. Biokhimiia},
  year={1999},
  volume={64 7},
  pages={817-23}
}
Bacteriophage T4 fibritin is a triple-stranded, parallel, segmented alpha-helical coiled-coil protein. Earlier we showed that the C-terminal globular domain (foldon) of fibritin is essential for correct trimerization and folding of the protein. We constructed the chimerical fusion protein W31 in which the fibritin foldon sequence is followed by the small globular non-alpha-helical protein gp31 of the T4 phage. We showed that the foldon is capable of trimerization in the absence of the coiled… CONTINUE READING

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References

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Showing 1-5 of 5 references

Evolutionary Biochem- istry and Related Areas of Physiocochemical Biology (Poglasov

  • B. N. Sobolev, M. M. Shneider, E. I. Marusich, V. V. Mesyanzhinov
  • eds.) Bach Institute of Biochem- istry and ANKO,
  • 1995
Highly Influential
4 Excerpts

Molecular Biology of Bacteriophage T4 (Karam, J. D., ed.) Ameri- can Society for Microbiology, Washington D.C

  • W. B. Wood, F. A. Eiserling
  • (Moscow) Vol
  • 1999
1 Excerpt

Protein Structure, Stability and Folding

  • Londer, Yu. Ya, V. V. Mesyanzhinov
  • Book of Program and Abstracts, ONTI PNC RAN…
  • 1998
1 Excerpt

Modelling of Structure of Bacte- riophage T4 Fibrillar Proteins: Candidate’s dissertation [in Russian], Ivanovsky Institute of Virology, Moscow

  • B. N. Sobolev
  • 1993
1 Excerpt

Molecular Cloning, Cold

  • J. Sambrook, E. F. Fritsch, T. Maniatis
  • 1989
2 Excerpts

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