1K1V
Solution Structure of the DNA-Binding Domain of MafG
Summary for 1K1V
| Entry DOI | 10.2210/pdb1k1v/pdb |
| Descriptor | MafG (1 entity in total) |
| Functional Keywords | maf, transcription factor, dna-binding domain, dna binding protein |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Nucleus (By similarity): O54790 |
| Total number of polymer chains | 1 |
| Total formula weight | 4962.73 |
| Authors | Kusunoki, H.,Motohashi, H.,Katsuoka, F.,Morohashi, A.,Yamamoto, M.,Tanaka, T. (deposition date: 2001-09-25, release date: 2002-04-10, Last modification date: 2024-05-29) |
| Primary citation | Kusunoki, H.,Motohashi, H.,Katsuoka, F.,Morohashi, A.,Yamamoto, M.,Tanaka, T. Solution structure of the DNA-binding domain of MafG. Nat.Struct.Biol., 9:252-256, 2002 Cited by PubMed Abstract: The Maf family proteins, which constitute a subgroup of basic region-leucine zipper (bZIP) proteins, function as transcriptional regulators of cellular differentiation. Together with the basic region, the Maf extended homology region (EHR), conserved only within the Maf family, defines the DNA binding specific to Mafs. Here we present the first NMR-derived structure of the DNA-binding domain (residues 1-76) of MafG, which contains the EHR and the basic region. The structure consists of three alpha-helices and resembles the fold of the DNA-binding domain of Skn-1, a developmental transcription factor of Caenorhabditis elegans. The structural similarity between MafG and Skn-1 enables us to propose a possible mechanism by which Maf family proteins recognize their consensus DNA sequences. PubMed: 11875518DOI: 10.1038/nsb771 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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