2eva
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Structural Basis for the Interaction of TAK1 Kinase with its Activating Protein TAB1
OverviewOverview
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.
About this StructureAbout this Structure
2EVA is a Single protein structure of sequence from Homo sapiens with as ligand. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for the interaction of TAK1 kinase with its activating protein TAB1., Brown K, Vial SC, Dedi N, Long JM, Dunster NJ, Cheetham GM, J Mol Biol. 2005 Dec 16;354(5):1013-20. Epub 2005 Nov 2. PMID:16289117
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