2EVA

Structural Basis for the Interaction of TAK1 Kinase with its Activating Protein TAB1

Summary for 2EVA

• Entry DOI: 10.2210/pdb2eva/pdb
• Descriptor: TAK1 kinase - TAB1 chimera fusion protein, ADENOSINE (3 entities in total)
• Functional Keywords: tak1, tab1, kinase, transferase-transferase activator complex, transferase/transferase activator
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm : O43318
• Total number of polymer chains: 1
• Total formula weight: 35048.35

Authors

Brown, K.,Vial, S.C.,Dedi, N.,Long, J.M.,Dunster, N.J.,Cheetham, G.M. (deposition date: 2005-10-31, release date: 2006-05-02, Last modification date: 2024-02-14)

Primary citation

Brown, K.,Vial, S.C.,Dedi, N.,Long, J.M.,Dunster, N.J.,Cheetham, G.M.
Structural basis for the interaction of TAK1 kinase with its activating protein TAB1
J.Mol.Biol., 354:1013-1020, 2005

PubMed 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.

PubMed: 16289117
DOI: 10.1016/j.jmb.2005.09.098

Experimental method

X-RAY DIFFRACTION (2 Å)