2vhf
From Proteopedia
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|PDB= 2vhf |SIZE=350|CAPTION= <scene name='initialview01'>2vhf</scene>, resolution 2.800Å | |PDB= 2vhf |SIZE=350|CAPTION= <scene name='initialview01'>2vhf</scene>, resolution 2.800Å | ||
|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> | |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> | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
| - | |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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1ixd|1IXD]], [[1whl|1WHL]], [[1whm|1WHM]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vhf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vhf OCA], [http://www.ebi.ac.uk/pdbsum/2vhf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2vhf RCSB]</span> | ||
}} | }} | ||
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[[Category: Scheel, H.]] | [[Category: Scheel, H.]] | ||
[[Category: Swift, S.]] | [[Category: Swift, S.]] | ||
| - | [[Category: ZN]] | ||
[[Category: alternative splicing]] | [[Category: alternative splicing]] | ||
[[Category: anti-oncogene]] | [[Category: anti-oncogene]] | ||
| Line 52: | Line 54: | ||
[[Category: zn-binding domain]] | [[Category: zn-binding domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:12:21 2008'' |
Revision as of 02:12, 31 March 2008
| |||||||
| , resolution 2.800Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , and | ||||||
| Ligands: | |||||||
| Activity: | Ubiquitin thiolesterase, with EC number 3.1.2.15 | ||||||
| Related: | 1IXD, 1WHL, 1WHM
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
Page seeded by OCA on Mon Mar 31 05:12:21 2008
Categories: Homo sapiens | Single protein | Ubiquitin thiolesterase | Ashworth, A. | Barford, D. | Hofmann, K. | Komander, D. | Lord, C J. | Scheel, H. | Swift, S. | Alternative splicing | Anti-oncogene | B-box | Cell cycle | Cell signalling | Cross-brace | Cytokine signalling | Cytoplasm | Deubiquitinating enzyme | Hydrolase | Linkage specificity | Lys63- linked | Nf-kb | Phosphorylation | Protease | Thiol protease | Ubiquitin | Ubl conjugation pathway | Usp domain | Zn-binding domain
