2WTY

Crystal structure of the homodimeric MafB in complex with the T-MARE binding site

Summary for 2WTY

• Entry DOI: 10.2210/pdb2wty/pdb
• Related: 2WT7
• Descriptor: TRANSCRIPTION FACTOR MAFB, DNA (5'-D(*TP*AP*AP*TP*TP*GP*CP*TP*GP*AP*CP*TP*CP*AP *GP*CP*AP*AP*AP*T)-3'), DNA (5'-D(*TP*AP*TP*TP*TP*GP*CP*TP*GP*AP*GP*TP*CP*AP *GP*CP*AP*AP*TP*T)-3'), ... (5 entities in total)
• Functional Keywords: repressor, dna-binding, transcription, proto-oncogene, transcription regulation, tumor suppressor, dna, b-zip, nucleus, activator, ap-1 binding site, protein-dna complex
• Biological source: MUS MUSCULUS (HOUSE MOUSE)
• Cellular location: Nucleus: P54841
• Total number of polymer chains: 4
• Total formula weight: 35675.18

Authors

Consani Textor, L.,Holton, S.,Wilmanns, M. (deposition date: 2009-09-25, release date: 2010-12-08, 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

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: 24530283
DOI: 10.1016/J.STR.2013.12.017

Experimental method

X-RAY DIFFRACTION (2.9 Å)