Characterization of an Additional Binding Surface on the p97 N-Terminal Domain Involved in Bipartite Cofactor Interactions.

@article{Hnzelmann2016CharacterizationOA,
  title={Characterization of an Additional Binding Surface on the p97 N-Terminal Domain Involved in Bipartite Cofactor Interactions.},
  author={Petra H{\"a}nzelmann and Hermann Schindelin},
  journal={Structure},
  year={2016},
  volume={24 1},
  pages={
          140-147
        }
}
The type II AAA ATPase p97 interacts with a large number of cofactors that regulate its function by recruiting it to different cellular pathways. Most of the cofactors interact with the N-terminal (N) domain of p97, either via ubiquitin-like domains or short linear binding motifs. While some linear binding motifs form α helices, another group features short stretches of unstructured hydrophobic sequences as found in the so-called SHP (BS1, binding segment 1) motif. Here we present the crystal… CONTINUE READING
BETA
Tweets
This paper has been referenced on Twitter 1 time. VIEW TWEETS

From This Paper

Figures, tables, and topics from this paper.

Citations

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

References

Publications referenced by this paper.
SHOWING 1-10 OF 44 REFERENCES

Similar Papers

Loading similar papers…