2b5m: Difference between revisions
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'''Crystal Structure of DDB1''' | '''Crystal Structure of DDB1''' | ||
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[[Category: Zheng, N.]] | [[Category: Zheng, N.]] | ||
[[Category: Zhou, P.]] | [[Category: Zhou, P.]] | ||
[[Category: | [[Category: Beta-propeller]] | ||
[[Category: | [[Category: Ddb1]] | ||
[[Category: | [[Category: Propeller cluster]] | ||
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Revision as of 19:53, 3 May 2008
Crystal Structure of DDB1
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
2B5M is a Single protein structure of sequence from Homo sapiens. 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 Page seeded by OCA on Sat May 3 19:53:08 2008