Crystal Structure of the Atypical Protein Kinase Domain of a TRP Channel
with Phosphotransferase Activity


Hiroto Yamaguchi, Masayuki Matsushita, Angus C. Nairn, and John Kuriyan

Molecular Cell, Vol 7, 1047-1057, May 2001

Figure from the paper / Crystal structure coordinates /

Summary

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.


Illustrations from the paper:

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Crystal Structure Coordinates:

Complex with ATP analog (AMP-PNP). PDB Code: 1IA9

Complex with ADP. PDB Code: 1IAH

Protein with no nucleotide PDB Code: 1IAJ