2h0d
From Proteopedia
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- | [[Image:2h0d.gif|left|200px]] | + | [[Image:2h0d.gif|left|200px]] |
- | + | ||
- | '''Structure of a Bmi-1-Ring1B Polycomb group ubiquitin ligase complex''' | + | {{Structure |
+ | |PDB= 2h0d |SIZE=350|CAPTION= <scene name='initialview01'>2h0d</scene>, resolution 2.50Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''Structure of a Bmi-1-Ring1B Polycomb group ubiquitin ligase complex''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 2H0D is a [ | + | 2H0D is a [[Protein complex]] structure of sequences 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=2H0D OCA]. |
==Reference== | ==Reference== | ||
- | Structure of a Bmi-1-Ring1B polycomb group ubiquitin ligase complex., Li Z, Cao R, Wang M, Myers MP, Zhang Y, Xu RM, J Biol Chem. 2006 Jul 21;281(29):20643-9. Epub 2006 May 18. PMID:[http:// | + | Structure of a Bmi-1-Ring1B polycomb group ubiquitin ligase complex., Li Z, Cao R, Wang M, Myers MP, Zhang Y, Xu RM, J Biol Chem. 2006 Jul 21;281(29):20643-9. Epub 2006 May 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16714294 16714294] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: transcription]] | [[Category: transcription]] | ||
[[Category: ubiquitin ligase]] | [[Category: ubiquitin ligase]] | ||
- | [[Category: | + | [[Category: wpigenetic]] |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:11:07 2008'' |
Revision as of 15:11, 20 March 2008
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, resolution 2.50Å | |||||||
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Coordinates: | save as pdb, mmCIF, xml |
Structure of a Bmi-1-Ring1B Polycomb group ubiquitin ligase complex
Overview
Polycomb group proteins Bmi-1 and Ring1B are core subunits of the PRC1 complex, which plays important roles in the regulation of Hox gene expression, X-chromosome inactivation, tumorigenesis, and stem cell self-renewal. The RING finger protein Ring1B is an E3 ligase that participates in the ubiquitination of lysine 119 of histone H2A, and the binding of Bmi-1 stimulates the E3 ligase activity. We have mapped the regions of Bmi-1 and Ring1B required for efficient ubiquitin transfer and determined a 2.5-A structure of the Bmi-1-Ring1B core domain complex. The structure reveals that Ring1B "hugs" Bmi-1 through extensive RING domain contacts and its N-terminal tail wraps around Bmi-1. The two regions of interaction have a synergistic effect on the E3 ligase activity. Our analyses suggest a model where the Bmi-1-Ring1B complex stabilizes the interaction between the E2 enzyme and the nucleosomal substrate to allow efficient ubiquitin transfer.
About this Structure
2H0D is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of a Bmi-1-Ring1B polycomb group ubiquitin ligase complex., Li Z, Cao R, Wang M, Myers MP, Zhang Y, Xu RM, J Biol Chem. 2006 Jul 21;281(29):20643-9. Epub 2006 May 18. PMID:16714294
Page seeded by OCA on Thu Mar 20 17:11:07 2008
Categories: Homo sapiens | Protein complex | Xu, R M. | ZN | Chromatin | Histone | Polycomb | Transcription | Ubiquitin ligase | Wpigenetic