Crystal structure of the atypical protein kinase domain of a TRP channel with phosphotransferase activity

Mol Cell. 2001 May;7(5):1047-57. doi: 10.1016/s1097-2765(01)00256-8.


Transient receptor potential (TRP) channels modulate calcium levels in eukaryotic cells in response to external signals. A novel transient receptor potential channel has the ability to phosphorylate itself and other proteins on serine and threonine residues. The catalytic domain of this channel kinase has no detectable sequence similarity to classical eukaryotic protein kinases and is essential for channel function. The structure of the kinase domain, reported here, reveals unexpected similarity to eukaryotic protein kinases in the catalytic core as well as to metabolic enzymes with ATP-grasp domains. The inclusion of the channel kinase catalytic domain within the eukaryotic protein kinase superfamily indicates a significantly wider distribution for this group of signaling proteins than suggested previously by sequence comparisons alone.

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Calcium Channels / chemistry*
  • Crystallography, X-Ray
  • Cyclic AMP-Dependent Protein Kinases / chemistry*
  • Evolution, Molecular
  • Mice
  • Models, Molecular
  • Molecular Sequence Data
  • Nucleotides / metabolism
  • Phosphotransferases / metabolism
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Sequence Alignment
  • TRPC Cation Channels
  • Zinc / metabolism


  • Calcium Channels
  • Nucleotides
  • TRPC Cation Channels
  • Phosphotransferases
  • Cyclic AMP-Dependent Protein Kinases
  • Zinc

Associated data

  • PDB/1IA9
  • PDB/1IAH
  • PDB/1IAJ