2eva: Difference between revisions

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[[Image:2eva.gif|left|200px]]
{{Seed}}
[[Image:2eva.png|left|200px]]


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{{STRUCTURE_2eva|  PDB=2eva  |  SCENE=  }}  
{{STRUCTURE_2eva|  PDB=2eva  |  SCENE=  }}  


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




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_16289117}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_16289117}}


==About this Structure==
==About this Structure==
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[[Category: Tab1]]
[[Category: Tab1]]
[[Category: Tak1]]
[[Category: Tak1]]
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