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Published on: March 22, 2012
Molecular basis for TANK recognition by TRAF1 revealed by the crystal structure of TRAF1/TANK complex
Chang Min Kim1, Jae-Hee Jeong2, Young-Jin Son3
1Department of Chemistry and Biochemistry, Graduate School of Biochemistry, Yeungnam University, Gyeongsan, South Korea.
Abstract:
Tumor necrosis factor receptor-associated factor 1 (TRAF1) is a multifunctional adaptor protein involved in important processes of cellular signaling, including innate immunity and apoptosis. TRAF family member-associated NF-kappaB activator (TANK) has been identified as a competitive intracellular inhibitor of TRAF2 function. Although TRAF recognition by various receptors has been studied extensively in the field of TRAF-mediated biology, molecular and functional details of TANK recognition and interaction with TRAF1 have not been studied. In this study, we report the crystal structure of the TRAF1/TANK peptide complex. Quantitative interaction experiments showed that TANK peptide interacts with both TRAF1 and TRAF2 with similar affinity in a micromolar range. Our structural study also reveals that TANK binds TRAF1 using a minor minimal consensus motif for TRAF binding, Px(Q/E)xT.
Database:
Coordinate and structural factor were deposited in the Protein Data Bank under PDB ID code 5H10.
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