2b5l | pdb_00002b5l

Crystal Structure of DDB1 In Complex with Simian Virus 5 V Protein

spinqualitylabelsall models 2b5l, resolution 2.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2b5l is a 4 chain structure with sequence from Human and Parainfluenza virus 5. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ZN Related: 2b5m, 2b5n Gene: P/V (Parainfluenza virus 5) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [V_SV5] Blocks host interferon signaling. Induces the ubiquitination and subsequent proteasome-mediated degradation of host STAT1. Acts as an adapter, linking host DDB1-Cullin 4 to STAT2/STAT1 complex. There is an absolute requirement of STAT2 in STAT1 degradation, as V binds specifically to STAT2. Might act as a chaperone keeping the viral nucleoprotein soluble. Interacts with host IFIH1/MDA5 to block its activity in the transduction pathway which leads to the activation of IFN-beta promoter, thus protecting the virus against cell antiviral state. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The DDB1-Cul4A ubiquitin ligase complex promotes protein ubiquitination in diverse cellular functions and is reprogrammed by the V proteins of paramyxoviruses to degrade STATs and block interferon signaling. Here we report the crystal structures of DDB1 alone and in complex with the simian virus 5 V protein. The DDB1 structure reveals an intertwined three-propeller cluster, which contains two tightly coupled beta propellers with a large pocket in between and a third beta propeller flexibly attached on the side. The rigid double-propeller fold of DDB1 is targeted by the viral V protein, which inserts an entire helix into the double-propeller pocket, whereas the third propeller domain docks DDB1 to the N terminus of the Cul4A scaffold. Together, these results not only provide structural insights into how the virus hijacks the DDB1-Cul4A ubiquitin ligase but also establish a structural framework for understanding the multiple functions of DDB1 in the uniquely assembled cullin-RING E3 machinery. Structure of DDB1 in complex with a paramyxovirus V protein: viral hijack of a propeller cluster in ubiquitin ligase.,Li T, Chen X, Garbutt KC, Zhou P, Zheng N Cell. 2006 Jan 13;124(1):105-17. PMID:16413485 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also DNA damage-binding protein Nonstructural protein

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