The modular structure of SIP facilitates its role in stabilizing multiprotein assemblies.

@article{Bhattacharya2005TheMS,
  title={The modular structure of SIP facilitates its role in stabilizing multiprotein assemblies.},
  author={Shibani Bhattacharya and Young-Tae Lee and Wojciech Michowski and Beata Jastrzebska and Anna Filipek and Jacek Kuźnicki and Walter J Chazin},
  journal={Biochemistry},
  year={2005},
  volume={44 27},
  pages={9462-71}
}
Siah-interacting protein (SIP) was identified as a novel adaptor that physically links the E3 ubiquitin ligase activity of Siah-1 with Skp1 and Ebi F-Box protein in the degradation of beta-catenin, a transcriptional activator of TCF/LEF genes. In this study, we have used solution NMR spectroscopy to characterize the domain structure of SIP, which includes a novel helical hairpin domain at the N-terminus flexibly linked to a CS domain and an unstructured carboxy terminal SGS domain. These… CONTINUE READING

From This Paper

Topics from this paper.
14 Citations
0 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 14 extracted citations

Similar Papers

Loading similar papers…