2h0d

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(New page: 200px<br /> <applet load="2h0d" size="450" color="white" frame="true" align="right" spinBox="true" caption="2h0d, resolution 2.50&Aring;" /> '''Structure of a Bmi-...)
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[[Image:2h0d.gif|left|200px]]<br />
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[[Image:2h0d.gif|left|200px]]<br /><applet load="2h0d" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="2h0d" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="2h0d, resolution 2.50&Aring;" />
caption="2h0d, resolution 2.50&Aring;" />
'''Structure of a Bmi-1-Ring1B Polycomb group ubiquitin ligase complex'''<br />
'''Structure of a Bmi-1-Ring1B Polycomb group ubiquitin ligase complex'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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2H0D is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2H0D OCA].
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2H0D is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H0D OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Xu, R.M.]]
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[[Category: Xu, R M.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: chromatin]]
[[Category: chromatin]]
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[[Category: wpigenetics]]
[[Category: wpigenetics]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:24:29 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:36:54 2008''

Revision as of 15:36, 21 February 2008

Image:2h0d.gif

2h0d, resolution 2.50Å

Drag the structure with the mouse to rotate

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 with as ligand. 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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