2WT7
Crystal structure of the bZIP heterodimeric complex MafB:cFos bound to DNA
Summary for 2WT7
| Entry DOI | 10.2210/pdb2wt7/pdb |
| Descriptor | PROTO-ONCOGENE PROTEIN C-FOS, TRANSCRIPTION FACTOR MAFB, MODIFIED T-MARE MOTIF, ... (6 entities in total) |
| Functional Keywords | transcription, transcription regulation, nucleus, activator, repressor, dna-binding, phosphoprotein, differentiation, tumor suppressor, proliferation, proto-oncogene |
| Biological source | MUS MUSCULUS (HOUSE MOUSE) More |
| Total number of polymer chains | 4 |
| Total formula weight | 28329.59 |
| Authors | Pogenberg, V.,Holton, S.,Wilmanns, M. (deposition date: 2009-09-11, release date: 2010-09-29, Last modification date: 2024-05-08) |
| Primary citation | Pogenberg, V.,Consani Textor, L.,Vanhille, L.,Holton, S.J.,Sieweke, M.H.,Wilmanns, M. Design of a bZIP Transcription Factor with Homo/Heterodimer-Induced DNA-Binding Preference. Structure, 22:466-, 2014 Cited by PubMed Abstract: The ability of basic leucine zipper transcription factors for homo- or heterodimerization provides a paradigm for combinatorial control of eukaryotic gene expression. It has been unclear, however, how facultative dimerization results in alternative DNA-binding repertoires on distinct regulatory elements. To unravel the molecular basis of such coupled preferences, we determined two high-resolution structures of the transcription factor MafB as a homodimer and as a heterodimer with c-Fos bound to variants of the Maf-recognition element. The structures revealed several unexpected and dimer-specific coiled-coil-heptad interactions. Based on these findings, we have engineered two MafB mutants with opposite dimerization preferences. One of them showed a strong preference for MafB/c-Fos heterodimerization and enabled selection of heterodimer-favoring over homodimer-specific Maf-recognition element variants. Our data provide a concept for transcription factor design to selectively activate dimer-specific pathways and binding repertoires. PubMed: 24530283DOI: 10.1016/J.STR.2013.12.017 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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