2FI2
Solution structure of the SCAN homodimer from MZF-1/ZNF42
Summary for 2FI2
| Entry DOI | 10.2210/pdb2fi2/pdb |
| NMR Information | BMRB: 6957 |
| Descriptor | Zinc finger protein 42 (1 entity in total) |
| Functional Keywords | scan domain, znf-42, mzf-1, homodimer, transcription factor, structural genomics, psi, protein structure initiative, center for eukaryotic structural genomics, cesg, transcription |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: P28698 |
| Total number of polymer chains | 2 |
| Total formula weight | 21035.78 |
| Authors | Volkman, B.F.,Peterson, F.C.,Sander, T.L.,Waltner, J.K.,Center for Eukaryotic Structural Genomics (CESG) (deposition date: 2005-12-27, release date: 2006-01-17, Last modification date: 2024-05-29) |
| Primary citation | Peterson, F.C.,Hayes, P.L.,Waltner, J.K.,Heisner, A.K.,Jensen, D.R.,Sander, T.L.,Volkman, B.F. Structure of the SCAN domain from the tumor suppressor protein MZF1. J.Mol.Biol., 363:137-147, 2006 Cited by PubMed Abstract: The SCAN domain mediates interactions between members of a subfamily of zinc-finger transcription factors and is found in more than 60 C2H2 zinc finger genes in the human genome, including the tumor suppressor gene myeloid zinc finger 1 (MZF1). Glutathione-S-transferase pull-down assays showed that the MZF1 SCAN domain self-associates, and a Kd value of 600 nM was measured by intrinsic tryptophan fluorescence polarization. The MZF1 structure determined by NMR spectroscopy revealed a domain-swapped dimer. Each monomer consists of five alpha helices in two subdomains connected by the alpha2-alpha3 loop. Residues from helix 3 of each monomer compose the core of the dimer interface, while the alpha1-alpha2 loop and helix 2 pack against helices 3 and 5 from the opposing monomer. Comprehensive sequence analysis is coupled with the first high-resolution structure of a SCAN dimer to provide an initial view of the recognition elements that govern dimerization for this large family of transcription factors. PubMed: 16950398DOI: 10.1016/j.jmb.2006.07.063 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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