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PDBsum entry 2b5l
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Protein binding/viral protein
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PDB id
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2b5l
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References listed in PDB file
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Key reference
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Title
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Structure of ddb1 in complex with a paramyxovirus v protein: viral hijack of a propeller cluster in ubiquitin ligase.
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Authors
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T.Li,
X.Chen,
K.C.Garbutt,
P.Zhou,
N.Zheng.
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Ref.
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Cell, 2006,
124,
105-117.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 3.
Figure 3. Multiple Potential Protein Interaction Sites Are
Found in the Double-Propeller Fold Formed by BPA and BPC of DDB1
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Figure 4.
Figure 4. Interactions between DDB1 and Cul4A Involve the
Top Surface of the DDB1 BPB Domain and a Conserved Sequence
Motif of Cul4A N-Terminal to the First Cullin Repeat
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The above figures are
reprinted
by permission from Cell Press:
Cell
(2006,
124,
105-117)
copyright 2006.
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