5C4V
Ski-like protein
Summary for 5C4V
| Entry DOI | 10.2210/pdb5c4v/pdb |
| Descriptor | Mothers against decapentaplegic homolog 4, Ski-like protein, GLYCEROL, ... (6 entities in total) |
| Functional Keywords | complex, signaling protein |
| Biological source | Homo sapiens (Human) More |
| Cellular location | Cytoplasm : Q13485 |
| Total number of polymer chains | 6 |
| Total formula weight | 129141.40 |
| Authors | Wallden, K.,Nyman, T.,Hallberg, B.M. (deposition date: 2015-06-18, release date: 2016-10-12, Last modification date: 2024-11-20) |
| Primary citation | Wallden, K.,Nyman, T.,Hallberg, B.M. SnoN Stabilizes the SMAD3/SMAD4 Protein Complex. Sci Rep, 7:46370-46370, 2017 Cited by PubMed Abstract: TGF-β 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-β 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-β signaling. PubMed: 28397834DOI: 10.1038/srep46370 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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