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| {{STRUCTURE_2pop| PDB=2pop | SCENE= }} | | {{STRUCTURE_2pop| PDB=2pop | SCENE= }} |
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| '''The Crystal Structure of TAB1 and BIR1 complex'''
| | ===The Crystal Structure of TAB1 and BIR1 complex=== |
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| ==Overview==
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| In addition to caspase inhibition, X-linked inhibitor of apoptosis (XIAP) induces NF-kappaB and MAP kinase activation during TGF-b and BMP receptor signaling and upon overexpression. Here we show that the BIR1 domain of XIAP, which has no previously ascribed function, directly interacts with TAB1 to induce NF-kappaB activation. TAB1 is an upstream adaptor for the activation of the kinase TAK1, which in turn couples to the NF-kappaB pathway. We report the crystal structures of BIR1, TAB1, and the BIR1/TAB1 complex. The BIR1/TAB1 structure reveals a striking butterfly-shaped dimer and the detailed interaction between BIR1 and TAB1. Structure-based mutagenesis and knockdown of TAB1 show unambiguously that the BIR1/TAB1 interaction is crucial for XIAP-induced TAK1 and NF-kappaB activation. We show that although not interacting with BIR1, Smac, the antagonist for caspase inhibition by XIAP, also inhibits the XIAP/TAB1 interaction. Disruption of BIR1 dimerization abolishes XIAP-mediated NF-kappaB activation, implicating a proximity-induced mechanism for TAK1 activation.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17560374}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17560374 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17560374}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Pp2c-like domain]] | | [[Category: Pp2c-like domain]] |
| [[Category: Zinc finger]] | | [[Category: Zinc finger]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 13:33:14 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:33:45 2008'' |
