3aqa: Difference between revisions

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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===
{{ABSTRACT_PUBMED_21513886}}


 
==Function==
<!--
[[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}}


==About this Structure==
==About this Structure==
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==Reference==
==Reference==
<ref group="xtra">PMID:021513886</ref><references group="xtra"/>
<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.]]
[[Category: Acetyl-lysine recognition]]
[[Category: Acetylated histone h4]]
[[Category: Helical bundle]]
[[Category: Nucleus]]
[[Category: Riken structural genomics/proteomics initiative]]
[[Category: Rsgi]]
[[Category: Structural genomic]]
[[Category: Transcription-transcription inhibitor complex]]

Revision as of 09:17, 27 March 2013

Template:STRUCTURE 3aqa

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

  1. 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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