7cby

Structure of FOXG1 DNA binding domain bound to DBE2 DNA site

spinqualitylabelsall models 7cby, resolution 1.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7cby is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.646Å Ligands: PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease FOXG1_HUMAN FOXG1 syndrome due to 14q12 microdeletion;14q11.2 microduplication syndrome. The disease is caused by variants affecting the gene represented in this entry. Function FOXG1_HUMAN Transcription repression factor which plays an important role in the establishment of the regional subdivision of the developing brain and in the development of the telencephalon. Publication Abstract from PubMed Forkhead box G1 (FOXG1) is a transcription factor mainly expressed in the brain that plays a critical role in the development and regionalization of the forebrain. Aberrant expression of FOXG1 has implications in FOXG1 syndrome, a serious neurodevelopmental disorder. Here, we report the crystal structure of the FOXG1 DNA-binding domain (DBD) in complex with the forkhead consensus DNA site DBE2 at the resolution of 1.6 A. FOXG1-DBD adopts a typical winged helix fold. Compared to those of other FOX-DBD/DBE2 structures, the N-terminus, H3 helix and wing2region of FOXG1-DBD exhibit differences in DNA recognition. The FOXG1-DBD wing2 region adopts a unique architecture composed of two beta-strands that differs from all other known FOX-DBD wing2 folds. Mutation assays revealed that the disease-causing mutations within the FOXG1-DBD affect DNA binding, protein thermal stability, or both. Our report provides initial insight into how FOXG1 binds DNA and sheds light on how disease-causing mutations in FOXG1-DBD affect its DNA-binding ability. Structural basis for DNA recognition by FOXG1 and the characterization of disease-causing FOXG1 mutations.,Dai S, Li J, Zhang H, Chen X, Guo M, Chen Z, Chen Y J Mol Biol. 2020 Oct 12. pii: S0022-2836(20)30583-0. doi:, 10.1016/j.jmb.2020.10.007. PMID:33058871 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also FOX 3D structures

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