Kim Chang Min, Jeong Jae-Hee, Son Young-Jin, Choi Jun-Hyuk, Kim Sunghwan, Park Hyun Ho
Department of Chemistry and Biochemistry, Graduate School of Biochemistry, Yeungnam University, Gyeongsan, South Korea.
Pohang Accelerator Laboratory, Pohang University of Science and Technology, South Korea.
FEBS Lett. 2017 Mar;591(5):810-821. doi: 10.1002/1873-3468.12584. Epub 2017 Feb 17.
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.
Coordinate and structural factor were deposited in the Protein Data Bank under PDB ID code 5H10.
肿瘤坏死因子受体相关因子1（TRAF1）是一种多功能衔接蛋白，参与细胞信号传导的重要过程，包括先天免疫和细胞凋亡。TRAF家族成员相关的NF-κB激活剂（TANK）已被鉴定为TRAF2功能的竞争性细胞内抑制剂。尽管在TRAF介导的生物学领域中，各种受体对TRAF的识别已得到广泛研究，但TANK与TRAF1识别和相互作用的分子及功能细节尚未得到研究。在本研究中，我们报道了TRAF1/TANK肽复合物的晶体结构。定量相互作用实验表明，TANK肽在微摩尔范围内以相似的亲和力与TRAF1和TRAF2相互作用。我们的结构研究还表明，TANK使用TRAF结合的最小共有基序Px(Q/E)xT与TRAF1结合。
坐标和结构因子已存入蛋白质数据库，登录号为PDB ID代码5H10。
