期刊
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
卷 21, 期 8, 页码 -出版社
MDPI
DOI: 10.3390/ijms21082895
关键词
apoptosis; inflammation; TRAF; TRADD; protein interaction
资金
- Basic Science Research Program of the National Research Foundation of Korea (NRF) - Korea government (MSIT) [NRF-2017M3A9D8062960, NRF-2018RIA2B2003635]
- Korea Healthcare Technology R&D Project, ministry of Health and Welfare, Republic of Korea [HI17C0155]
Although TRAF1 and TRAF2 share common receptors and have extremely conserved amino acid residues, recent studies have shown that key differences in receptor binding preferences with different affinities exist, which might be important for their different functions in TRAF-mediated signal transduction. To better understand TRAF1 and TRAF2 signaling, we analyzed and compared their receptor binding-affinities. Our study revealed that TRADD, TANK, and caspase-2 bind to both TRAF1 and TRAF2 with different affinities in vitro. Sequence and structural analyses revealed that S454 on TRAF2 (corresponding to A369 of TRAF1) is critical for the binding of TRADD, and F347 on TRAF1 (corresponding to L432 of TRAF2) is a critical determinant for high affinity binding of TANK and caspase-2.
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