共查询到20条相似文献,搜索用时 0 毫秒
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Nan Chai Wan-Xin Li Jue Wang Zhi-Xin Wang Shi-Ming Yang Jia-Wei Wu 《Nucleic acids research》2015,43(18):9051-9064
Smad proteins are important intracellular mediators of TGF-β signalling, which transmit signals directly from cell surface receptors to the nucleus. The MH1 domain of Smad plays a key role in DNA recognition. Two types of DNA sequence were identified as Smad binding motifs: the Smad binding element (SBE) and the GC-rich sequence. Here we report the first crystal structure of the Smad5 MH1 domain in complex with the GC-rich sequence. Compared with the Smad5-MH1/SBE complex structure, the Smad5 MH1 domain contacts the GC-rich site with the same β-hairpin, but the detailed interaction modes are different. Conserved β-hairpin residues make base specific contacts with the minimal GC-rich site, 5′-GGC-3′. The assembly of Smad5-MH1 on the GC-rich DNA also results in distinct DNA conformational changes. Moreover, the crystal structure of Smad5-MH1 in complex with a composite DNA sequence demonstrates that the MH1 domain is targeted to each binding site (GC-rich or SBE) with modular binding modes, and the length of the DNA spacer affects the MH1 assembly. In conclusion, our work provides the structural basis for the recognition and binding specificity of the Smad MH1 domain with the DNA targets. 相似文献
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Regulation of Smad7 promoter by direct association with Smad3 and Smad4 总被引:26,自引:0,他引:26
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Pax3 and regulation of the melanocyte-specific tyrosinase-related protein-1 promoter. 总被引:8,自引:0,他引:8
M D Galibert U Yavuzer T J Dexter C R Goding 《The Journal of biological chemistry》1999,274(38):26894-26900
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PIAS1 interacts with and represses SOX9 transactivation activity 总被引:1,自引:0,他引:1
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Smad6 is a Smad1/5-induced smad inhibitor. Characterization of bone morphogenetic protein-responsive element in the mouse Smad6 promoter 总被引:7,自引:0,他引:7
Ishida W Hamamoto T Kusanagi K Yagi K Kawabata M Takehara K Sampath TK Kato M Miyazono K 《The Journal of biological chemistry》2000,275(9):6075-6079
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Kim MY Jung J Mo JS Ann EJ Ahn JS Yoon JH Park HS 《Experimental cell research》2011,317(17):2438-2446
Notch signaling involves the proteolytic cleavage of the transmembrane Notch receptor after binding to its transmembrane ligands. Jagged-1 also undergoes proteolytic cleavage by gamma-secretase and releases an intracellular fragment. In this study, we have demonstrated that the Jagged-1 intracellular domain (JICD) inhibits Notch1 signaling via a reduction in the protein stability of the Notch1 intracellular domain (Notch1-IC). The formation of the Notch1-IC-RBP-Jk-Mastermind complex is prevented in the presence of JICD, via a physical interaction. Furthermore, JICD accelerates the protein degradation of Notch1-IC via Fbw7-dependent proteasomal pathway. These results indicate that JICD functions as a negative regulator in Notch1 signaling via the promotion of Notch1-IC degradation. 相似文献