6dat

ETS1 in complex with synthetic SRR mimic

spinqualitylabelsall models 6dat, resolution 2.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6dat is a 6 chain structure with sequence from Mus musculus and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3500264Å Ligands: NH2, PF5, SEP, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ETS1_MOUSE Transcription factor. Publication Abstract from PubMed The eukaryotic transcription factor ETS1 is regulated by an intrinsically disordered serine-rich region (SRR) that transiently associates with the adjacent ETS domain to inhibit DNA binding. In this study, we further elucidated the physicochemical basis for ETS1 autoinhibition by characterizing the interaction of its ETS domain with a series of synthetic peptides corresponding to the SRR. Binding is driven by the hydrophobic effect and enhanced electrostatically by phosphorylation of serines adjacent to aromatic residues in the amphipathic SRR. Structural characterization of the dynamic peptide/protein complex by NMR spectroscopy and X-ray crystallography revealed multiple modes of binding that lead to autoinhibition by synergistically blocking the DNA-binding interface of the ETS domain and stabilizing an appended helical inhibitory module against allosterically induced unfolding. Consistent with these conclusions, the SRR peptide does not interact with DNA-bound ETS1. In addition, we found that the ETS1 SRR phosphopeptide binds to distantly-related PU.1 in vitro, indicating autoinhibition exploits features of the ETS domain that are conserved across this family of transcription factors. The Biophysical Basis for Phosphorylation-Enhanced DNA-Binding Autoinhibition of the ETS1 Transcription Factor.,Perez-Borrajero C, Lin CS, Okon M, Scheu K, Graves BJ, Murphy MEP, McIntosh LP J Mol Biol. 2018 Dec 28. pii: S0022-2836(18)31286-5. doi:, 10.1016/j.jmb.2018.12.011. PMID:30597162 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ets1

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