5GN0
Structure of TAZ-TEAD complex
Summary for 5GN0
| Entry DOI | 10.2210/pdb5gn0/pdb |
| Descriptor | Transcriptional enhancer factor TEF-3, WW domain-containing transcription regulator protein 1, CITRIC ACID, ... (5 entities in total) |
| Functional Keywords | transcription |
| Biological source | Mus musculus (Mouse) More |
| Cellular location | Nucleus: Q62296 Q9EPK5 |
| Total number of polymer chains | 8 |
| Total formula weight | 123151.67 |
| Authors | Kaan, H.Y.K.,Song, H. (deposition date: 2016-07-18, release date: 2017-05-31, Last modification date: 2024-11-20) |
| Primary citation | Kaan, H.Y.K.,Chan, S.W.,Tan, S.K.J.,Guo, F.,Lim, C.J.,Hong, W.,Song, H. Crystal structure of TAZ-TEAD complex reveals a distinct interaction mode from that of YAP-TEAD complex Sci Rep, 7:2035-2035, 2017 Cited by PubMed Abstract: The Hippo pathway is a tumor suppressor pathway that is implicated in the regulation of organ size. The pathway has three components: the upstream regulatory factors, the kinase core, and the downstream transcriptional machinery, which consists of YAP, TAZ (transcription co-activators) and TEAD (transcription factor). Formation of YAP/TAZ-TEAD complexes leads to the transcription of growth-promoting genes. Herein, we report the crystal structure of TAZ-TEAD4 complex, which reveals two binding modes. The first is similar to the published YAP-TEAD structure. The second is a unique binding mode, whereby two molecules of TAZ bind to and bridge two molecules of TEAD4. We validated the latter using cross-linking and multi-angle light scattering. Using siRNA, we showed that TAZ knockdown leads to a decrease in TEAD4 dimerization. Lastly, results from luciferase assays, using YAP/TAZ transfected or knockdown cells, give support to the non-redundancy of YAP/TAZ co-activators in regulating gene expression in the Hippo pathway. PubMed: 28515457DOI: 10.1038/s41598-017-02219-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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