2vhf

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(New page: 200px<br /><applet load="2vhf" size="350" color="white" frame="true" align="right" spinBox="true" caption="2vhf, resolution 2.800&Aring;" /> '''STRUCTURE OF THE CY...)
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[[Image:2vhf.jpg|left|200px]]<br /><applet load="2vhf" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2vhf.jpg|left|200px]]
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caption="2vhf, resolution 2.800&Aring;" />
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'''STRUCTURE OF THE CYLD USP DOMAIN'''<br />
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{{Structure
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|PDB= 2vhf |SIZE=350|CAPTION= <scene name='initialview01'>2vhf</scene>, resolution 2.800&Aring;
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|SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Zn+Binding+Site+For+Chain+A'>AC2</scene>, <scene name='pdbsite=AC3:Zn+Binding+Site+For+Chain+B'>AC3</scene> and <scene name='pdbsite=AC4:Zn+Binding+Site+For+Chain+B'>AC4</scene>
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|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Ubiquitin_thiolesterase Ubiquitin thiolesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.15 3.1.2.15]
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|GENE=
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}}
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'''STRUCTURE OF THE CYLD USP DOMAIN'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2VHF 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=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Ubiquitin_thiolesterase Ubiquitin thiolesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.15 3.1.2.15] Known structural/functional Sites: <scene name='pdbsite=AC1:Zn+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Zn+Binding+Site+For+Chain+A'>AC2</scene>, <scene name='pdbsite=AC3:Zn+Binding+Site+For+Chain+B'>AC3</scene> and <scene name='pdbsite=AC4:Zn+Binding+Site+For+Chain+B'>AC4</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VHF OCA].
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2VHF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VHF OCA].
==Reference==
==Reference==
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The Structure of the CYLD USP Domain Explains Its Specificity for Lys63-Linked Polyubiquitin and Reveals a B Box Module., Komander D, Lord CJ, Scheel H, Swift S, Hofmann K, Ashworth A, Barford D, Mol Cell. 2008 Feb 29;29(4):451-64. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18313383 18313383]
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The Structure of the CYLD USP Domain Explains Its Specificity for Lys63-Linked Polyubiquitin and Reveals a B Box Module., Komander D, Lord CJ, Scheel H, Swift S, Hofmann K, Ashworth A, Barford D, Mol Cell. 2008 Feb 29;29(4):451-64. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18313383 18313383]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: zn-binding domain]]
[[Category: zn-binding domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Mar 14 09:35:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:46:38 2008''

Revision as of 16:46, 20 March 2008

Image:2vhf.jpg


PDB ID 2vhf

Drag the structure with the mouse to rotate
, resolution 2.800Å
Sites: , , and
Ligands:
Activity: Ubiquitin thiolesterase, with EC number 3.1.2.15
Coordinates: save as pdb, mmCIF, xml



STRUCTURE OF THE CYLD USP DOMAIN


Overview

The tumor suppressor CYLD antagonizes NF-kappaB and JNK signaling by disassembly of Lys63-linked ubiquitin chains synthesized in response to cytokine stimulation. Here we describe the crystal structure of the CYLD USP domain, revealing a distinctive architecture that provides molecular insights into its specificity toward Lys63-linked polyubiquitin. We identify regions of the USP domain responsible for this specificity and demonstrate endodeubiquitinase activity toward such chains. Pathogenic truncations of the CYLD C terminus, associated with the hypertrophic skin tumor cylindromatosis, disrupt the USP domain, accounting for loss of CYLD catalytic activity. A small zinc-binding B box domain, similar in structure to other crossbrace Zn-binding folds-including the RING domain found in E3 ubiquitin ligases-is inserted within the globular core of the USP domain. Biochemical and functional characterization of the B box suggests a role as a protein-interaction module that contributes to determining the subcellular localization of CYLD.

About this Structure

2VHF is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The Structure of the CYLD USP Domain Explains Its Specificity for Lys63-Linked Polyubiquitin and Reveals a B Box Module., Komander D, Lord CJ, Scheel H, Swift S, Hofmann K, Ashworth A, Barford D, Mol Cell. 2008 Feb 29;29(4):451-64. PMID:18313383

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