1IAJ

CRYSTAL STRUCTURE OF THE ATYPICAL PROTEIN KINASE DOMAIN OF A TRP CA-CHANNEL, CHAK (APO)

Summary for 1IAJ

• Entry DOI: 10.2210/pdb1iaj/pdb
• Related: 1IA9 1IAH
• Descriptor: TRANSIENT RECEPTOR POTENTIAL-RELATED PROTEIN, ZINC ION (2 entities in total)
• Functional Keywords: alpha/beta, protein kinase like fold, atp-grasp fold, transferase
• Biological source: Mus musculus (house mouse)
• Cellular location: Membrane; Multi-pass membrane protein (Probable): Q923J1
• Total number of polymer chains: 2
• Total formula weight: 64624.56

Authors

Yamaguchi, H.,Matsushita, M.,Nairn, A.C.,Kuriyan, J. (deposition date: 2001-03-22, release date: 2001-06-06, Last modification date: 2024-02-07)

Primary citation

Yamaguchi, H.,Matsushita, M.,Nairn, A.C.,Kuriyan, J.
Crystal structure of the atypical protein kinase domain of a TRP channel with phosphotransferase activity.
Mol.Cell, 7:1047-1057, 2001

PubMed 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.

PubMed: 11389851
DOI: 10.1016/S1097-2765(01)00256-8

Experimental method

X-RAY DIFFRACTION (2.8 Å)