User:Benjamin Elliott/Crystal Structure of the Bromodomain-PHD Finger Module of Human Transcriptional Co-Activator CBP in complex with Acetylated Histone 4 Peptide (H4K20ac)
From Proteopedia
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from the acetylated lysine. | from the acetylated lysine. | ||
| + | Unlike other BrDs that preferentially bind to diacetylated regions of the histone<ref>DOI 10.1016/j.cell.2012.02.013</ref><ref>DOI | ||
== Disease== | == Disease== | ||
In the larger complex, this domain functions as the domain that binds directly to the histone protein when it recognizes acetylation. Alterations in the of the human CBP gene results have been implicated in hematological malignancies as well as congenital malformation and mental retardation<ref>PMID 9613201</ref>. | In the larger complex, this domain functions as the domain that binds directly to the histone protein when it recognizes acetylation. Alterations in the of the human CBP gene results have been implicated in hematological malignancies as well as congenital malformation and mental retardation<ref>PMID 9613201</ref>. | ||
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There are two different sections which are missing electron density in their region, which suggests a high degree of structural mobility in solution. These regions are from <scene name='76/769329/1212-1253/1'>residue 1212 to 1253</scene> and <scene name='76/769329/Short_unshown_chain/1'>1261 to 1269</scene>. Though unshown in the crystal structure, the lack of electron density associated with such a lack of imaging suggests a high degree of structural mobility through these sections. | There are two different sections which are missing electron density in their region, which suggests a high degree of structural mobility in solution. These regions are from <scene name='76/769329/1212-1253/1'>residue 1212 to 1253</scene> and <scene name='76/769329/Short_unshown_chain/1'>1261 to 1269</scene>. Though unshown in the crystal structure, the lack of electron density associated with such a lack of imaging suggests a high degree of structural mobility through these sections. | ||
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| - | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | ||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 00:37, 10 October 2017
4N3W at Resolution 1.9 Å
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References
- ↑ Sanchez R, Meslamani J, Zhou MM. The bromodomain: from epigenome reader to druggable target. Biochim Biophys Acta. 2014 Aug;1839(8):676-85. doi: 10.1016/j.bbagrm.2014.03.011., Epub 2014 Mar 28. PMID:24686119 doi:http://dx.doi.org/10.1016/j.bbagrm.2014.03.011
- ↑ Plotnikov AN, Yang S, Zhou TJ, Rusinova E, Frasca A, Zhou MM. Structural Insights into Acetylated-Histone H4 Recognition by the Bromodomain-PHD Finger Module of Human Transcriptional Coactivator CBP. Structure. 2013 Dec 18. pii: S0969-2126(13)00437-1. doi:, 10.1016/j.str.2013.10.021. PMID:24361270 doi:http://dx.doi.org/10.1016/j.str.2013.10.021
- ↑ Filippakopoulos P, Picaud S, Mangos M, Keates T, Lambert JP, Barsyte-Lovejoy D, Felletar I, Volkmer R, Muller S, Pawson T, Gingras AC, Arrowsmith CH, Knapp S. Histone recognition and large-scale structural analysis of the human bromodomain family. Cell. 2012 Mar 30;149(1):214-31. PMID:22464331 doi:10.1016/j.cell.2012.02.013
- ↑ Unknown PubmedID ==Disease==Inthelargercomplex,thisdomainfunctionsasthedomainthatbindsdirectlytothehistoneproteinwhenitrecognizesacetylation.AlterationsintheofthehumanCBPgeneresultshavebeenimplicatedinhematologicalmalignanciesaswellascongenitalmalformationandmentalretardation<ref>PMID9613201</li> <li id="cite_note-4">[[#cite_ref-4|↑]] Park S, Martinez-Yamout MA, Dyson HJ, Wright PE. The CH2 domain of CBP/p300 is a novel zinc finger. FEBS Lett. 2013 Aug 19;587(16):2506-11. doi: 10.1016/j.febslet.2013.06.051. Epub , 2013 Jul 4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/23831576 23831576] doi:[http://dx.doi.org/10.1016/j.febslet.2013.06.051 http://dx.doi.org/10.1016/j.febslet.2013.06.051]</li></ol></ref>
