2h0d: Difference between revisions
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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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| 2h0d, resolution 2.50Å | |||||||||||||
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| Ligands: | ZN | ||||||||||||
| 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
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