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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<StructureSection load='4n3w' size='340' side='right' caption='Generic view of BrD-PHD finger module bound to H4K20ac' scene=''> | <StructureSection load='4n3w' size='340' side='right' caption='Generic view of BrD-PHD finger module bound to H4K20ac' scene=''> | ||
'''4N3W''' is a 2-domain complex of a bromodomain (BrD) and a plant homeodomain (PHD) that functions in humans to recognize the epigenetic acetylation of histones. | '''4N3W''' is a 2-domain complex of a bromodomain (BrD) and a plant homeodomain (PHD) that functions in humans to recognize the epigenetic acetylation of histones. | ||
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| - | This is a default text for your page '''Benjamin Elliott/Crystal Structure of the Bromodomain-PHD Finger Module of Human Transcriptional Co-Activator CBP in complex with Acetylated Histone 4 Peptide (H4K20ac)'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
| - | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||
== Function == | == Function == | ||
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This protein is composed of two different domains -- the bromodomain (BrD) and the plant homeodomain (PHD) finger. In this particular module for human CBP, the two come together to form such interactions that they function as a single structural unit.There are two <scene name='76/769329/Zinc_ions/1'>zinc ion coordination centers</scene> that serve as a stable base for an extended interface established between the PHD finger and the BrD. The PHD finger itself has not shown to bind any specific peptide, whether in tandem or in its individual construct. The separation of the domains is shown <scene name='76/769329/Annoying_one/2'>here</scene>, with the BrD shown in aquamarine, the PHD finger shown in red, and the linkers of the two domains shown in blue. | This protein is composed of two different domains -- the bromodomain (BrD) and the plant homeodomain (PHD) finger. In this particular module for human CBP, the two come together to form such interactions that they function as a single structural unit.There are two <scene name='76/769329/Zinc_ions/1'>zinc ion coordination centers</scene> that serve as a stable base for an extended interface established between the PHD finger and the BrD. The PHD finger itself has not shown to bind any specific peptide, whether in tandem or in its individual construct. The separation of the domains is shown <scene name='76/769329/Annoying_one/2'>here</scene>, with the BrD shown in aquamarine, the PHD finger shown in red, and the linkers of the two domains shown in blue. | ||
| + | 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, | ||
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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> | ||
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. | 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. | ||
Revision as of 14:57, 5 October 2017
4N3W at Resolution 1.9 Å
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References
- ↑ 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
