2b5n: Difference between revisions

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New page: left|200px<br /><applet load="2b5n" size="450" color="white" frame="true" align="right" spinBox="true" caption="2b5n, resolution 2.8Å" /> '''Crystal Structure of ...
 
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[[Image:2b5n.gif|left|200px]]<br /><applet load="2b5n" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2b5n.gif|left|200px]]<br /><applet load="2b5n" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2b5n, resolution 2.8&Aring;" />
caption="2b5n, resolution 2.8&Aring;" />
'''Crystal Structure of the DDB1 BPB Domain'''<br />
'''Crystal Structure of the DDB1 BPB Domain'''<br />


==Overview==
==Overview==
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.
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 Structure==
==About this Structure==
2B5N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with IPA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2B5N OCA].  
2B5N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=IPA:'>IPA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B5N OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Chen, X.]]
[[Category: Chen, X.]]
[[Category: Garbutt, K.C.]]
[[Category: Garbutt, K C.]]
[[Category: Li, T.]]
[[Category: Li, T.]]
[[Category: Zheng, N.]]
[[Category: Zheng, N.]]
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[[Category: propeller cluster]]
[[Category: propeller cluster]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:34:32 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:34:26 2008''

Revision as of 17:34, 21 February 2008

File:2b5n.gif


2b5n, resolution 2.8Å

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Crystal Structure of the DDB1 BPB Domain

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

2B5N is a Single protein structure of sequence from Homo sapiens with 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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