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| | {{STRUCTURE_2hye| PDB=2hye | SCENE= }} | | {{STRUCTURE_2hye| PDB=2hye | SCENE= }} |
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| - | '''Crystal Structure of the DDB1-Cul4A-Rbx1-SV5V Complex'''
| + | ===Crystal Structure of the DDB1-Cul4A-Rbx1-SV5V Complex=== |
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| - | ==Overview==
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| - | Protein ubiquitination is a common form of post-translational modification that regulates a broad spectrum of protein substrates in diverse cellular pathways. Through a three-enzyme (E1-E2-E3) cascade, the attachment of ubiquitin to proteins is catalysed by the E3 ubiquitin ligase, which is best represented by the superfamily of the cullin-RING complexes. Conserved from yeast to human, the DDB1-CUL4-ROC1 complex is a recently identified cullin-RING ubiquitin ligase, which regulates DNA repair, DNA replication and transcription, and can also be subverted by pathogenic viruses to benefit viral infection. Lacking a canonical SKP1-like cullin adaptor and a defined substrate recruitment module, how the DDB1-CUL4-ROC1 E3 apparatus is assembled for ubiquitinating various substrates remains unclear. Here we present crystallographic analyses of the virally hijacked form of the human DDB1-CUL4A-ROC1 machinery, which show that DDB1 uses one beta-propeller domain for cullin scaffold binding and a variably attached separate double-beta-propeller fold for substrate presentation. Through tandem-affinity purification of human DDB1 and CUL4A complexes followed by mass spectrometry analysis, we then identify a novel family of WD40-repeat proteins, which directly bind to the double-propeller fold of DDB1 and serve as the substrate-recruiting module of the E3. Together, our structural and proteomic results reveal the structural mechanisms and molecular logic underlying the assembly and versatility of a new family of cullin-RING E3 complexes.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16964240}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16964240 is the PubMed ID number. |
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| | ==Disease== | | ==Disease== |
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| | [[Category: Ring finger]] | | [[Category: Ring finger]] |
| | [[Category: Zinc finger]] | | [[Category: Zinc finger]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:51:49 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:35:58 2008'' |
Revision as of 17:36, 27 July 2008
Template:STRUCTURE 2hye
Crystal Structure of the DDB1-Cul4A-Rbx1-SV5V Complex
Template:ABSTRACT PUBMED 16964240
Disease
Known disease associated with this structure: Xeroderma pigmentosum, group E, subtype 2 OMIM:[600045]
About this Structure
2HYE is a Protein complex structure of sequences from Homo sapiens and Simian virus 5. Full crystallographic information is available from OCA.
Reference
Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase machinery., Angers S, Li T, Yi X, MacCoss MJ, Moon RT, Zheng N, Nature. 2006 Oct 5;443(7111):590-3. PMID:16964240
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