8RIT
Dimeric mutant S103D of the BTB domain of ZBTB8A from Xenopus laevis
Summary for 8RIT
| Entry DOI | 10.2210/pdb8rit/pdb |
| Descriptor | Zinc finger and BTB domain-containing protein 8A.1-A (1 entity in total) |
| Functional Keywords | transcription regulation, btb domain, polymerisation, transcription |
| Biological source | Xenopus laevis (African clawed frog) |
| Total number of polymer chains | 6 |
| Total formula weight | 105707.81 |
| Authors | Coste, F.,Suskiewicz, M.J. (deposition date: 2023-12-19, release date: 2024-06-05, Last modification date: 2024-12-18) |
| Primary citation | Mance, L.,Bigot, N.,Zhamungui Sanchez, E.,Coste, F.,Martin-Gonzalez, N.,Zentout, S.,Biliskov, M.,Pukalo, Z.,Mishra, A.,Chapuis, C.,Arteni, A.A.,Lateur, A.,Goffinont, S.,Gaudon, V.,Talhaoui, I.,Casuso, I.,Beaufour, M.,Garnier, N.,Artzner, F.,Cadene, M.,Huet, S.,Castaing, B.,Suskiewicz, M.J. Dynamic BTB-domain filaments promote clustering of ZBTB proteins. Mol.Cell, 84:2490-2510.e9, 2024 Cited by PubMed Abstract: The formation of dynamic protein filaments contributes to various biological functions by clustering individual molecules together and enhancing their binding to ligands. We report such a propensity for the BTB domains of certain proteins from the ZBTB family, a large eukaryotic transcription factor family implicated in differentiation and cancer. Working with Xenopus laevis and human proteins, we solved the crystal structures of filaments formed by dimers of the BTB domains of ZBTB8A and ZBTB18 and demonstrated concentration-dependent higher-order assemblies of these dimers in solution. In cells, the BTB-domain filamentation supports clustering of full-length human ZBTB8A and ZBTB18 into dynamic nuclear foci and contributes to the ZBTB18-mediated repression of a reporter gene. The BTB domains of up to 21 human ZBTB family members and two related proteins, NACC1 and NACC2, are predicted to behave in a similar manner. Our results suggest that filamentation is a more common feature of transcription factors than is currently appreciated. PubMed: 38996459DOI: 10.1016/j.molcel.2024.05.029 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.75 Å) |
Structure validation
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