5vpc

Transcription factor FosB/JunD bZIP domain in its oxidized form, type-II crystal

spinqualitylabelsall models 5vpc, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5vpc is a 4 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 2.498Å Ligands: CL, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FOSB_HUMAN FosB interacts with Jun proteins enhancing their DNA binding activity. Publication Abstract from PubMed The transcription factor, activator protein-1 (AP-1), binds to cognate DNA under redox control; yet, the underlying mechanism has remained enigmatic. A series of crystal structures of the AP-1 FosB/JunD bZIP domains reveal ordered DNA-binding regions in both FosB and JunD even in absence DNA. However, while JunD is competent to bind DNA, the FosB bZIP domain must undergo a large conformational rearrangement that is controlled by a 'redox switch' centered on an inter-molecular disulfide bond. Solution studies confirm that FosB/JunD cannot undergo structural transition and bind DNA when the redox-switch is in the 'OFF' state, and show that the mid-point redox potential of the redox switch affords it sensitivity to cellular redox homeostasis. The molecular and structural studies presented here thus reveal the mechanism underlying redox-regulation of AP-1 Fos/Jun transcription factors and provide structural insight for therapeutic interventions targeting AP-1 proteins. Activator Protein-1: redox switch controlling structure and DNA-binding.,Yin Z, Machius M, Nestler EJ, Rudenko G Nucleic Acids Res. 2017 Sep 7. doi: 10.1093/nar/gkx795. PMID:28981703 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Metallothiol transferase FosB

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