2b5l
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Crystal Structure of DDB1 In Complex with Simian Virus 5 V Protein
OverviewOverview
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.
About this StructureAbout this Structure
2B5L is a Protein complex structure of sequences from Homo sapiens and Simian virus 40 with ZN as ligand. Full crystallographic information is available from OCA.
ReferenceReference
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
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