2b5l

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(New page: 200px<br /><applet load="2b5l" size="450" color="white" frame="true" align="right" spinBox="true" caption="2b5l, resolution 2.85&Aring;" /> '''Crystal Structure of...)
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[[Image:2b5l.gif|left|200px]]<br /><applet load="2b5l" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:2b5l.gif|left|200px]]<br /><applet load="2b5l" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2b5l, resolution 2.85&Aring;" />
caption="2b5l, resolution 2.85&Aring;" />
'''Crystal Structure of DDB1 In Complex with Simian Virus 5 V Protein'''<br />
'''Crystal Structure of DDB1 In Complex with Simian Virus 5 V Protein'''<br />
==Overview==
==Overview==
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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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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==
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2B5L is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Simian_virus_40 Simian virus 40] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2B5L OCA].
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2B5L is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Simian_virus_40 Simian virus 40] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B5L OCA].
==Reference==
==Reference==
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[[Category: Simian virus 40]]
[[Category: Simian virus 40]]
[[Category: Chen, X.]]
[[Category: Chen, X.]]
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[[Category: Garbutt, K.C.]]
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[[Category: Garbutt, K C.]]
[[Category: Li, T.]]
[[Category: Li, T.]]
[[Category: Zheng, N.]]
[[Category: Zheng, N.]]
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[[Category: zinc finger]]
[[Category: zinc finger]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:34:25 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:34:24 2008''

Revision as of 14:34, 21 February 2008


2b5l, resolution 2.85Å

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

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.

About this Structure

2B5L is a Protein complex structure of sequences from Homo sapiens and Simian virus 40 with as ligand. Full crystallographic information is available from OCA.

Reference

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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