Defining a pathway of communication from the C-terminal peptide binding domain to the N-terminal ATPase domain in a AAA protein.

@article{Cashikar2002DefiningAP,
  title={Defining a pathway of communication from the C-terminal peptide binding domain to the N-terminal ATPase domain in a AAA protein.},
  author={Anil G. Cashikar and Eric C Schirmer and Douglas A. Hattendorf and John R. Glover and M. S. Ramakrishnan and Danielle M Ware and Susan L. Lindquist},
  journal={Molecular cell},
  year={2002},
  volume={9 4},
  pages={751-60}
}
AAA proteins remodel other proteins to affect a multitude of biological processes. Their power to remodel substrates must lie in their capacity to couple substrate binding to conformational changes via cycles of nucleotide binding and hydrolysis, but these relationships have not yet been deciphered for any member. We report that when one AAA protein, Hsp104, engages polypeptide at the C-terminal peptide-binding region, the ATPase cycle of the C-terminal nucleotide-binding domain (NBD2) drives a… CONTINUE READING
Highly Influential
This paper has highly influenced 10 other papers. REVIEW HIGHLY INFLUENTIAL CITATIONS

From This Paper

Figures, tables, and topics from this paper.

Citations

Publications citing this paper.
Showing 1-10 of 51 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 38 references

Global unfolding of a substrate protein by the Hsp 100 chap - 13203 – 13208 . erone ClpA

  • A. J. Wilkinson
  • Nature
  • 2001

Similar Papers

Loading similar papers…