2h0d: Difference between revisions
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'''Structure of a Bmi-1-Ring1B Polycomb group ubiquitin ligase complex''' | '''Structure of a Bmi-1-Ring1B Polycomb group ubiquitin ligase complex''' | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Xu, R M.]] | [[Category: Xu, R M.]] | ||
[[Category: | [[Category: Chromatin]] | ||
[[Category: | [[Category: Histone]] | ||
[[Category: | [[Category: Polycomb]] | ||
[[Category: | [[Category: Transcription]] | ||
[[Category: | [[Category: Ubiquitin ligase]] | ||
[[Category: | [[Category: Wpigenetic]] | ||
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Revision as of 02:43, 4 May 2008
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 Sun May 4 05:43:13 2008
