Solution structure of the dimeric SAM domain of MAPKKK Ste11 and its interactions with the adaptor protein Ste50 from the budding yeast: implications for Ste11 activation and signal transmission through the Ste50-Ste11 complex.

@article{Bhattacharjya2004SolutionSO,
  title={Solution structure of the dimeric SAM domain of MAPKKK Ste11 and its interactions with the adaptor protein Ste50 from the budding yeast: implications for Ste11 activation and signal transmission through the Ste50-Ste11 complex.},
  author={Surajit Bhattacharjya and Ping Xu and Richard Gingras and Rustem Shaykhutdinov and Cunle Wu and Malcolm Whiteway and Feng Ni},
  journal={Journal of molecular biology},
  year={2004},
  volume={344 4},
  pages={1071-87}
}
Ste11, a homologue of mammalian MAPKKKs, together with its binding partner Ste50 works in a number of MAPK signaling pathways of Saccharomyces cerevisiae. Ste11/Ste50 binding is mediated by their sterile alpha motifs or SAM domains, of which homologues are also found in many other intracellular signaling and regulatory proteins. Here, we present the solution structure of the SAM domain or residues D37-R104 of Ste11 and its interactions with the cognate SAM domain-containing region of Ste50… CONTINUE READING

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