Identification of dimer interactions required for the catalytic activity of the TRPM7 alpha-kinase domain.

@article{Crawley2009IdentificationOD,
  title={Identification of dimer interactions required for the catalytic activity of the TRPM7 alpha-kinase domain.},
  author={Scott William Crawley and Graham P. C{\^o}t{\'e}},
  journal={The Biochemical journal},
  year={2009},
  volume={420 1},
  pages={
          115-22
        }
}
TRPM7 (transient receptor potential melastatin) combines an ion channel domain with a C-terminal protein kinase domain that belongs to the atypical alpha-kinase family. The TRPM7 alpha-kinase domain assembles into a dimer through the exchange of an N-terminal segment that extends from residue 1551 to residue 1577 [Yamaguchi, Matsushita, Nairn and Kuriyan (2001) Mol. Cell 7, 1047-1057]. Here, we show, by analysis of truncation mutants, that residues 1553-1562 of the N-terminus are essential for… CONTINUE READING

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