5v3m

mouseZFP568-ZnF1-11 in complex with DNA

spinqualitylabelsall models 5v3m, resolution 2.09Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5v3m is a 3 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.091Å Ligands: ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ZN568_MOUSE Has transcriptional repression activity, partially through the recruitment of the corepressor TRIM28 but has also repression activity independently of this interaction (PubMed:22110054, PubMed:27658112). Essential during embryonic development, where it acts as direct repressor of IGF2-P0, placental-specific transcript of IGF2, in early development and regulates convergent extension movements required for axis elongation and tissue morphogenesis in all germ layers (PubMed:18701545, PubMed:22110054, PubMed:28522536). Also important for normal morphogenesis of extraembryonic tissues including the yolk sac, extraembryonic mesoderm and placenta (PubMed:18701545, PubMed:21094155). May enhance proliferation or maintenance of neural stem cells (PubMed:23071813). Publication Abstract from PubMed Tandem zinc finger (ZF) proteins are the largest and most rapidly diverging family of DNA-binding transcription regulators in mammals. ZFP568 represses a transcript of placental-specific insulin like growth factor 2 (Igf2-P0) in mice. ZFP568 binds a 24-base pair sequence-specific element upstream of Igf2-P0 via the eleven-ZF array. Both DNA and protein conformations deviate from the conventional one finger-three bases recognition, with individual ZFs contacting 2, 3, or 4 bases and recognizing thymine on the opposite strand. These interactions arise from a shortened minor groove caused by an AT-rich stretch, suggesting adaptability of ZF arrays to sequence variations. Despite conservation in mammals, mutations at Igf2 and ZFP568 reduce their binding affinity in chimpanzee and humans. Our studies provide important insights into the evolutionary and structural dynamics of ZF-DNA interactions that play a key role in mammalian development and evolution. DNA Conformation Induces Adaptable Binding by Tandem Zinc Finger Proteins.,Patel A, Yang P, Tinkham M, Pradhan M, Sun MA, Wang Y, Hoang D, Wolf G, Horton JR, Zhang X, Macfarlan T, Cheng X Cell. 2018 Mar 22;173(1):221-233.e12. doi: 10.1016/j.cell.2018.02.058. Epub 2018 , Mar 15. PMID:29551271 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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