Abstract
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.
Keywords
BiologyProtein kinase domainCell biologyBiochemistryc-RafMAP2K7KinaseProtein kinase ACyclin-dependent kinase 2Mutant
MeSH Terms
Amino Acid MotifsAmino Acid SequenceAnimalsBinding SitesCalcium ChannelsCrystallographyX-RayCyclic AMP-Dependent Protein KinasesEvolutionMolecularMiceModelsMolecularMolecular Sequence DataNucleotidesPhosphotransferasesProtein StructureSecondaryProtein StructureTertiarySequence AlignmentTRPC Cation ChannelsZinc
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Publication Info
- Year
- 2001
- Type
- article
- Volume
- 7
- Issue
- 5
- Pages
- 1047-1057
- Citations
- 269
- Access
- Closed
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Cite This
Hiroto Yamaguchi,
Masayuki Matsushita,
Angus C. Nairn
et al.
(2001).
Crystal Structure of the Atypical Protein Kinase Domain of a TRP Channel with Phosphotransferase Activity.
Molecular Cell
, 7
(5)
, 1047-1057.
https://doi.org/10.1016/s1097-2765(01)00256-8
Identifiers
- DOI
- 10.1016/s1097-2765(01)00256-8
- PMID
- 11389851