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3aqa

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[[Image:3aqa.jpg|left|200px]]
 
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{{STRUCTURE_3aqa| PDB=3aqa | SCENE= }}
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===Crystal structure of the human BRD2 BD1 bromodomain in complex with a BRD2-interactive compound, BIC1===
===Crystal structure of the human BRD2 BD1 bromodomain in complex with a BRD2-interactive compound, BIC1===
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{{ABSTRACT_PUBMED_21513886}}
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==Function==
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[[http://www.uniprot.org/uniprot/BRD2_HUMAN BRD2_HUMAN]] May play a role in spermatogenesis or folliculogenesis (By similarity). Binds hyperacetylated chromatin and plays a role in the regulation of transcription, probably by chromatin remodeling. Regulates transcription of the CCND1 gene. Plays a role in nucleosome assembly.<ref>PMID:18406326</ref>
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{{ABSTRACT_PUBMED_21513886}}
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==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:021513886</ref><references group="xtra"/>
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<ref group="xtra">PMID:021513886</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Nakamura, Y.]]
[[Category: Nakamura, Y.]]
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[[Category: Umehara, T.]]
[[Category: Umehara, T.]]
[[Category: Yokoyama, S.]]
[[Category: Yokoyama, S.]]
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[[Category: Acetyl-lysine recognition]]
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[[Category: Acetylated histone h4]]
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[[Category: Helical bundle]]
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[[Category: Nucleus]]
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[[Category: Riken structural genomics/proteomics initiative]]
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[[Category: Rsgi]]
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[[Category: Structural genomic]]
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[[Category: Transcription-transcription inhibitor complex]]

Revision as of 09:17, 27 March 2013

Template:STRUCTURE 3aqa

Contents

Crystal structure of the human BRD2 BD1 bromodomain in complex with a BRD2-interactive compound, BIC1

Template:ABSTRACT PUBMED 21513886

Function

[BRD2_HUMAN] May play a role in spermatogenesis or folliculogenesis (By similarity). Binds hyperacetylated chromatin and plays a role in the regulation of transcription, probably by chromatin remodeling. Regulates transcription of the CCND1 gene. Plays a role in nucleosome assembly.[1]

About this Structure

3aqa is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Ito T, Umehara T, Sasaki K, Nakamura Y, Nishino N, Terada T, Shirouzu M, Padmanabhan B, Yokoyama S, Ito A, Yoshida M. Real-Time Imaging of Histone H4K12-Specific Acetylation Determines the Modes of Action of Histone Deacetylase and Bromodomain Inhibitors. Chem Biol. 2011 Apr 22;18(4):495-507. PMID:21513886 doi:10.1016/j.chembiol.2011.02.009
  1. ↑ LeRoy G, Rickards B, Flint SJ. The double bromodomain proteins Brd2 and Brd3 couple histone acetylation to transcription. Mol Cell. 2008 Apr 11;30(1):51-60. doi: 10.1016/j.molcel.2008.01.018. PMID:18406326 doi:10.1016/j.molcel.2008.01.018

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