Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

7QQD

Nuclear factor one X - NFIX in P21

Summary for 7QQD
Entry DOI10.2210/pdb7qqd/pdb
DescriptorNuclear factor 1 X-type, NFI binding site (forward), NFI binding site (reverse), ... (6 entities in total)
Functional Keywordstranscription factor, nfi, nfix, nf-1, dna binding protein
Biological sourceHomo sapiens (human)
More
Total number of polymer chains4
Total formula weight48834.95
Authors
Lapi, M.,Chaves-Sanjuan, A.,Gourlay, L.J.,Tiberi, M.,Polentarutti, M.,Demitri, N.,Bais, G.,Nardini, M. (deposition date: 2022-01-07, release date: 2023-01-18, Last modification date: 2025-12-24)
Primary citationTiberi, M.,Lapi, M.,Gourlay, L.J.,Chaves-Sanjuan, A.,Polentarutti, M.,Demitri, N.,Cavinato, M.,Bonnet, D.M.V.,Taglietti, V.,Righetti, A.,Sala, R.,Cauteruccio, S.,Kumawat, A.,Russo, R.,Barbiroli, A.G.,Gnesutta, N.,Camilloni, C.,Bolognesi, M.,Messina, G.,Nardini, M.
Structural basis of Nuclear Factor 1-X DNA recognition provides prototypic insight into the NFI family.
Nat Commun, 16:10170-10170, 2025
Cited by
PubMed Abstract: Nuclear Factor I (NFI) proteins are involved in adenovirus DNA replication and regulate gene transcription, stem cell proliferation, and differentiation. They play key roles in development, cancer, and congenital disorders. Within the NFI family, NFI-X is critical for neural stem cell biology, hematopoiesis, muscle development, muscular dystrophies, and oncogenesis. Here, we present the structural characterization of the NFI transcription factor NFI-X, both alone and bound to its consensus palindromic DNA site. Our analyses reveal a MH1-like fold within NFI-X DNA-binding domain (DBD) and identify crucial structural determinants for activity, such as a Zn²⁺ binding site, dimeric assembly, and DNA-binding specificity. Given the ~85% sequence identity within the NFI DBDs, our structural data are prototypic for the entire family, a NFI Rosetta Stone that allows decoding a wealth of biochemical and functional data and provides a precise target for drug design in a wider disease context.
PubMed: 41261119
DOI: 10.1038/s41467-025-65186-0
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.7 Å)
Structure validation

249697

PDB entries from 2026-02-25

PDB statisticsPDBj update infoContact PDBjnumon