3aqa
From Proteopedia
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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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==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
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
- ↑ 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
Categories: Homo sapiens | Nakamura, Y. | Padmanabhan, B. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Shirouzu, M. | Terada, T. | Umehara, T. | Yokoyama, S. | Acetyl-lysine recognition | Acetylated histone h4 | Helical bundle | Nucleus | Riken structural genomics/proteomics initiative | Rsgi | Structural genomic | Transcription-transcription inhibitor complex