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10.1038/srep46370 http://scihub22266oqcxt.onion/10.1038/srep46370 C5387736!5387736 !28397834     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28397834 &cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\28397834 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Sci+Rep 2017 ; 7 (ä): 46370 Nephropedia Template TP {{tp|p=28397834 |t=2017. SnoN Stabilizes the SMAD3/SMAD4 Protein Complex |pdf=|usr=}}{{28397834 }} gab.com Text SnoN Stabilizes the SMAD3/SMAD4 Protein Complex JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=28397834 #FOAvip TGF-? signaling regulates cellular processes such as proliferation, differentiation and apoptosis through activation of SMAD transcription factors that are in turn modulated by members of the Ski-SnoN family. In this process, Ski has been shown to negatively modulate TGF-? signaling by disrupting active R-SMAD/Co-SMAD heteromers. Here, we show that the related regulator SnoN forms a stable complex with the R-SMAD (SMAD3) and the Co-SMAD (SMAD4). To rationalize this stabilization at the molecular level, we determined the crystal structure of a complex between the SAND domain of SnoN and the MH2-domain of SMAD4. This structure shows a binding mode that is compatible with simultaneous coordination of R-SMADs. Our results show that SnoN, and SMAD heteromers can form a joint structural core for the binding of other transcription modulators. The results are of fundamental importance for our understanding of the molecular mechanisms behind the modulation of TGF-? signaling. Twit Text FOAVip SnoN Stabilizes the SMAD3/SMAD4 Protein Complex ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=28397834 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28397834 #FOAvip English Wikipedia <ref>{{Cite pmid|28397834 }}</ref> SnoN Stabilizes the SMAD3/SMAD4 Protein Complex #MMPMID28397834 Walldén K ; Nyman T ; Hällberg BM Sci Rep 2017[Apr]; 7 (ä): 46370 PMID28397834 show ga TGF-? signaling regulates cellular processes such as proliferation, differentiation and apoptosis through activation of SMAD transcription factors that are in turn modulated by members of the Ski-SnoN family. In this process, Ski has been shown to negatively modulate TGF-? signaling by disrupting active R-SMAD/Co-SMAD heteromers. Here, we show that the related regulator SnoN forms a stable complex with the R-SMAD (SMAD3) and the Co-SMAD (SMAD4). To rationalize this stabilization at the molecular level, we determined the crystal structure of a complex between the SAND domain of SnoN and the MH2-domain of SMAD4. This structure shows a binding mode that is compatible with simultaneous coordination of R-SMADs. Our results show that SnoN, and SMAD heteromers can form a joint structural core for the binding of other transcription modulators. The results are of fundamental importance for our understanding of the molecular mechanisms behind the modulation of TGF-? signaling. |Humans [MESH] |Intracellular Signaling Peptides and Proteins/*metabolism [MESH] |Models, Molecular [MESH] |Protein Binding [MESH] |Protein Conformation [MESH] |Proto-Oncogene Proteins/*metabolism [MESH] |Signal Transduction/physiology [MESH] |Smad3 Protein/*metabolism [MESH]SnoN Stabilizes the SMAD3/SMAD4 Protein Complex (epmc).pdf DeepDyve Pubget Overpricing