Summary for 3L2C
Entry DOI | 10.2210/pdb3l2c/pdb |
Descriptor | FOXO consensus binding sequence, plus strand, FOXO consensus binding sequence, minus strand, Forkhead box protein O4, ... (5 entities in total) |
Functional Keywords | forkhead, forkhead box, winged helix, transcription-dna complex, transcription/dna |
Biological source | Homo sapiens (human) More |
Cellular location | Cytoplasm: P98177 |
Total number of polymer chains | 3 |
Total formula weight | 20265.58 |
Authors | Boura, E.,Silhan, J.,Sulc, M.,Brynda, J.,Obsilova, V.,Obsil, T. (deposition date: 2009-12-15, release date: 2009-12-29, Last modification date: 2023-11-01) |
Primary citation | Boura, E.,Rezabkova, L.,Brynda, J.,Obsilova, V.,Obsil, T. Structure of the human FOXO4-DBD-DNA complex at 1.9 A resolution reveals new details of FOXO binding to the DNA Acta Crystallogr.,Sect.D, 66:1351-1357, 2010 Cited by PubMed Abstract: FOXO4 is a member of the FOXO subgroup of forkhead transcription factors that constitute key components of a conserved signalling pathway that connects growth and stress signals to transcriptional control. Here, the 1.9 Å resolution crystal structure of the DNA-binding domain of human FOXO4 (FOXO4-DBD) bound to a 13 bp DNA duplex containing a FOXO consensus binding sequence is reported. The structure shows a similar recognition of the core sequence as has been shown for two other FOXO proteins. Helix H3 is docked into the major groove and provides all of the base-specific contacts, while the N-terminus and wing W1 make additional contacts with the phosphate groups of DNA. In contrast to other FOXO-DBD-DNA structures, the loop between helices H2 and H3 has a different conformation and participates in DNA binding. In addition, the structure of the FOXO4-DBD-DNA complex suggests that both direct water-DNA base contacts and the unique water-network interactions contribute to FOXO-DBD binding to the DNA in a sequence-specific manner. PubMed: 21123876DOI: 10.1107/S0907444910042228 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.868 Å) |
Structure validation
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