3i3j
From Proteopedia
(Difference between revisions)
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<StructureSection load='3i3j' size='340' side='right'caption='[[3i3j]], [[Resolution|resolution]] 2.33Å' scene=''> | <StructureSection load='3i3j' size='340' side='right'caption='[[3i3j]], [[Resolution|resolution]] 2.33Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[3i3j]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3i3j]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3I3J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3I3J FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.33Å</td></tr> |
- | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
- | < | + | |
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3i3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i3j OCA], [https://pdbe.org/3i3j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3i3j RCSB], [https://www.ebi.ac.uk/pdbsum/3i3j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3i3j ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3i3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i3j OCA], [https://pdbe.org/3i3j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3i3j RCSB], [https://www.ebi.ac.uk/pdbsum/3i3j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3i3j ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
- | + | [https://www.uniprot.org/uniprot/EP300_HUMAN EP300_HUMAN] Note=Defects in EP300 may play a role in epithelial cancer. Note=Chromosomal aberrations involving EP300 may be a cause of acute myeloid leukemias. Translocation t(8;22)(p11;q13) with KAT6A. Defects in EP300 are the cause of Rubinstein-Taybi syndrome type 2 (RSTS2) [MIM:[https://omim.org/entry/613684 613684]. A disorder characterized by craniofacial abnormalities, postnatal growth deficiency, broad thumbs, broad big toes, mental retardation and a propensity for development of malignancies. Some individuals with RSTS2 have less severe mental impairment, more severe microcephaly, and a greater degree of changes in facial bone structure than RSTS1 patients.<ref>PMID:15706485</ref> | |
== Function == | == Function == | ||
- | + | [https://www.uniprot.org/uniprot/EP300_HUMAN EP300_HUMAN] Functions as histone acetyltransferase and regulates transcription via chromatin remodeling. Acetylates all four core histones in nucleosomes. Histone acetylation gives an epigenetic tag for transcriptional activation. Mediates cAMP-gene regulation by binding specifically to phosphorylated CREB protein. Also functions as acetyltransferase for nonhistone targets. Acetylates 'Lys-131' of ALX1 and acts as its coactivator in the presence of CREBBP. Acetylates SIRT2 and is proposed to indirectly increase the transcriptional activity of TP53 through acetylation and subsequent attenuation of SIRT2 deacetylase function. Acetylates HDAC1 leading to its inactivation and modulation of transcription. Acts as a TFAP2A-mediated transcriptional coactivator in presence of CITED2. Plays a role as a coactivator of NEUROD1-dependent transcription of the secretin and p21 genes and controls terminal differentiation of cells in the intestinal epithelium. Promotes cardiac myocyte enlargement. Can also mediate transcriptional repression. Binds to and may be involved in the transforming capacity of the adenovirus E1A protein. In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes. Acetylates FOXO1 and enhances its transcriptional activity.<ref>PMID:11701890</ref> <ref>PMID:10733570</ref> <ref>PMID:11430825</ref> <ref>PMID:12586840</ref> <ref>PMID:12929931</ref> <ref>PMID:15186775</ref> <ref>PMID:15890677</ref> <ref>PMID:16762839</ref> <ref>PMID:18722353</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Homo sapiens]] |
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[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Arrowsmith | + | [[Category: Arrowsmith CH]] |
- | [[Category: Bountra | + | [[Category: Bountra C]] |
- | [[Category: Chaikuad | + | [[Category: Chaikuad A]] |
- | + | [[Category: Edwards AM]] | |
- | [[Category: Edwards | + | [[Category: Filippakopoulos P]] |
- | [[Category: Filippakopoulos | + | [[Category: Knapp S]] |
- | [[Category: Knapp | + | [[Category: Muniz J]] |
- | [[Category: Muniz | + | [[Category: Phillips C]] |
- | [[Category: Phillips | + | [[Category: Picaud S]] |
- | [[Category: Picaud | + | [[Category: Pike ACW]] |
- | [[Category: Pike | + | [[Category: Roos A]] |
- | [[Category: Roos | + | [[Category: Weigelt J]] |
- | + | [[Category: Von Delft F]] | |
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Current revision
Crystal Structure of the Bromodomain of Human EP300
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Categories: Homo sapiens | Large Structures | Arrowsmith CH | Bountra C | Chaikuad A | Edwards AM | Filippakopoulos P | Knapp S | Muniz J | Phillips C | Picaud S | Pike ACW | Roos A | Weigelt J | Von Delft F