Polymerization of the SAM domain of MAPKKK Ste11 from the budding yeast: implications for efficient signaling through the MAPK cascades.

@article{Bhattacharjya2005PolymerizationOT,
  title={Polymerization of the SAM domain of MAPKKK Ste11 from the budding yeast: implications for efficient signaling through the MAPK cascades.},
  author={Surajit Bhattacharjya and Ping Xu and Mukundan Chakrapani and Linda Johnston and Feng Ni},
  journal={Protein science : a publication of the Protein Society},
  year={2005},
  volume={14 3},
  pages={828-35}
}
The sterile alpha-motif (SAM) is a protein module approximately 70 residues long and mainly involved in the protein-protein interactions of cell signaling and transcriptional repression. The SAM domain of the yeast MAPKKK Ste11 has a well-folded dimeric structure in solution. Interestingly, the well-folded dimer of the Ste11 SAM undergoes a time-dependent self-assembly upon lowering of the pH, leading to the formation of high molecular weight oligomers. The oligomeric structures rapidly… CONTINUE READING

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