Comparison of Target Recognition by TRAF1 and TRAF2
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 transductio...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2020-04-01
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| Series: | International Journal of Molecular Sciences |
| Subjects: | |
| Online Access: | https://www.mdpi.com/1422-0067/21/8/2895 |
| _version_ | 1797570125380976640 |
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| author | Chang Min Kim Hyun Ho Park |
| author_facet | Chang Min Kim Hyun Ho Park |
| author_sort | Chang Min Kim |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-10T20:20:29Z |
| format | Article |
| id | doaj.art-9a2bc85c789a4b15819d4120a7295b96 |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-10T20:20:29Z |
| publishDate | 2020-04-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-9a2bc85c789a4b15819d4120a7295b962023-11-19T22:15:29ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672020-04-01218289510.3390/ijms21082895Comparison of Target Recognition by TRAF1 and TRAF2Chang Min Kim0Hyun Ho Park1College of Pharmacy, Chung-Ang University, Dongjag-gu, Seoul 06974, KoreaCollege of Pharmacy, Chung-Ang University, Dongjag-gu, Seoul 06974, KoreaAlthough 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.https://www.mdpi.com/1422-0067/21/8/2895apoptosisinflammationTRAFTRADDprotein interaction |
| spellingShingle | Chang Min Kim Hyun Ho Park Comparison of Target Recognition by TRAF1 and TRAF2 International Journal of Molecular Sciences apoptosis inflammation TRAF TRADD protein interaction |
| title | Comparison of Target Recognition by TRAF1 and TRAF2 |
| title_full | Comparison of Target Recognition by TRAF1 and TRAF2 |
| title_fullStr | Comparison of Target Recognition by TRAF1 and TRAF2 |
| title_full_unstemmed | Comparison of Target Recognition by TRAF1 and TRAF2 |
| title_short | Comparison of Target Recognition by TRAF1 and TRAF2 |
| title_sort | comparison of target recognition by traf1 and traf2 |
| topic | apoptosis inflammation TRAF TRADD protein interaction |
| url | https://www.mdpi.com/1422-0067/21/8/2895 |
| work_keys_str_mv | AT changminkim comparisonoftargetrecognitionbytraf1andtraf2 AT hyunhopark comparisonoftargetrecognitionbytraf1andtraf2 |