Deciphering the cross talk between hnRNP K and c-Src: the c-Src activation domain in hnRNP K is distinct from a second interaction site.

@article{Adolph2007DecipheringTC,
  title={Deciphering the cross talk between hnRNP K and c-Src: the c-Src activation domain in hnRNP K is distinct from a second interaction site.},
  author={D{\"o}rte Adolph and Nadine Flach and Katharina Mueller and Dirk H. Ostareck and Antje Ostareck-Lederer},
  journal={Molecular and cellular biology},
  year={2007},
  volume={27 5},
  pages={
          1758-70
        }
}
The protein tyrosine kinase c-Src is regulated by two intramolecular interactions. The repressed state is achieved through the interaction of the Src homology 2 (SH2) domain with the phosphorylated C-terminal tail and the association of the SH3 domain with a polyproline type II helix formed by the linker region between SH2 and the kinase domain. hnRNP K, the founding member of the KH domain protein family, is involved in chromatin remodeling, regulation of transcription, and translation of… CONTINUE READING
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