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. 2005 Dec 16;354(5):1013-20.
doi: 10.1016/j.jmb.2005.09.098. Epub 2005 Nov 2.

Structural basis for the interaction of TAK1 kinase with its activating protein TAB1

Kieron Brown  1 , Sarah C M Vial, Neesha Dedi, Joanna M Long, Nicholas J Dunster, Graham M T Cheetham
Affiliations

Structural basis for the interaction of TAK1 kinase with its activating protein TAB1

Kieron Brown et al. J Mol Biol. .

Abstract

Transforming growth factor-beta (TGF-beta)-activated kinase 1 (TAK1) is a member of the MAPKKK family of protein kinases, and is involved in intracellular signalling pathways stimulated by transforming growth factor beta, interleukin-1 and tumour necrosis factor-alpha. TAK1 is known to rely upon an additional protein, TAK1-binding protein 1 (TAB1), for complete activation. However, the molecular basis for this activation has yet to be elucidated. We have solved the crystal structure of a novel TAK1 chimeric protein and these data give insight into how TAK1 is activated by TAB1. Our results reveal a novel binding pocket on the TAK1 kinase domain whose shape complements that of a unique alpha-helix in the TAK1 binding domain of TAB1, providing the basis for an intimate hydrophobic association between the protein activator and its target.

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