1IAH

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

1IAH の概要

• エントリーDOI: 10.2210/pdb1iah/pdb
• 関連するPDBエントリー: 1IA9 1IAJ
• 分子名称: TRANSIENT RECEPTOR POTENTIAL-RELATED PROTEIN, ZINC ION, ADENOSINE-5'-DIPHOSPHATE, ... (6 entities in total)
• 機能のキーワード: alpha/beta, protein kinase like fold, atp-grasp fold, transferase
• 由来する生物種: Mus musculus (house mouse)
• 細胞内の位置: Membrane; Multi-pass membrane protein (Probable): Q923J1
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 65657.52

構造登録者

Yamaguchi, H.,Matsushita, M.,Nairn, A.C.,Kuriyan, J. (登録日: 2001-03-22, 公開日: 2001-06-06, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.4 Å)