6uls - Revision history

OCA at 07:54, 11 October 2023

2023-10-11T07:54:07Z

←Older revision		Revision as of 07:54, 11 October 2023
Line 1:		Line 1:

-	====	+	==BRD4-BD1 in complex with the a diacetylated-E2F1 peptide==
-	<StructureSection load='6uls' size='340' side='right'caption='[[6uls]]' scene=''>	+	<StructureSection load='6uls' size='340' side='right'caption='[[6uls]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6uls]] is a 2 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=6ULS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ULS FirstGlance]. <br>
-	</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=6uls FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uls OCA], [https://pdbe.org/6uls PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6uls RCSB], [https://www.ebi.ac.uk/pdbsum/6uls PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6uls ProSAT]</span></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.5Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</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=6uls FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uls OCA], [https://pdbe.org/6uls PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6uls RCSB], [https://www.ebi.ac.uk/pdbsum/6uls PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6uls ProSAT]</span></td></tr>
	</table>		</table>
		+	== Disease ==
		+	[https://www.uniprot.org/uniprot/BRD4_HUMAN BRD4_HUMAN] Note=A chromosomal aberration involving BRD4 is found in a rare, aggressive, and lethal carcinoma arising in midline organs of young people. Translocation t(15;19)(q14;p13) with NUT which produces a BRD4-NUT fusion protein.<ref>PMID:12543779</ref> <ref>PMID:11733348</ref>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/BRD4_HUMAN BRD4_HUMAN] Plays a role in a process governing chromosomal dynamics during mitosis (By similarity).
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Almost all eukaryotic proteins receive diverse post-translational modifications (PTMs) that modulate protein activity. Many histone PTMs are well characterized, heavily influence gene regulation, and are often predictors of distinct transcriptional programs. Although our understanding of the histone PTM network has matured, much is yet to be understood about the roles of transcription factor (TF) PTMs, which might well represent a similarly complex and dynamic network of functional regulation. Members of the bromodomain and extra-terminal domain (BET) family of proteins recognize acetyllysine residues and relay the signals encoded by these modifications. Here, we have investigated the acetylation dependence of several functionally relevant BET-TF interactions in vitro using surface plasmon resonance, nuclear magnetic resonance, and X-ray crystallography. We show that motifs known to be acetylated in TFs E2F1 and MyoD1 can interact with all bromodomains of BRD2, BRD3, and BRD4. The interactions are dependent on diacetylation of the motifs and show a preference for the first BET bromodomain. Structural mapping of the interactions confirms a conserved mode of binding for the two TFs to the acetyllysine binding pocket of the BET bromodomains, mimicking that of other already established functionally important histone- and TF-BET interactions. We also examined a motif from the TF RelA that is known to be acetylated but were unable to observe any interaction, regardless of the acetylation state of the sequence. Our findings overall advance our understanding of BET-TF interactions and suggest a physical link between the important diacetylated motifs found in E2F1 and MyoD1 and the BET-family proteins.
		+
		+	BET-Family Bromodomains Can Recognize Diacetylated Sequences from Transcription Factors Using a Conserved Mechanism.,Patel K, Solomon PD, Walshe JL, Ford DJ, Wilkinson-White L, Payne RJ, Low JKK, Mackay JP Biochemistry. 2021 Mar 9;60(9):648-662. doi: 10.1021/acs.biochem.0c00816. Epub , 2021 Feb 23. PMID:33620209<ref>PMID:33620209</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6uls" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Bromodomain-containing protein 3D structures\|Bromodomain-containing protein 3D structures]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Z-disk~~]]	+	[[Category: Low JKK]]
		+	[[Category: Mackay JP]]
		+	[[Category: Patel K]]

OCA at 14:56, 3 March 2021

2021-03-03T14:56:20Z

←Older revision		Revision as of 14:56, 3 March 2021
Line 3:		Line 3:
	<StructureSection load='6uls' size='340' side='right'caption='[[6uls]]' scene=''>		<StructureSection load='6uls' size='340' side='right'caption='[[6uls]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br>	+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=6uls FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uls OCA], [~~http~~://pdbe.org/6uls PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6uls RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6uls PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6uls ProSAT]</span></td></tr>	+	</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=6uls FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uls OCA], [https://pdbe.org/6uls PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6uls RCSB], [https://www.ebi.ac.uk/pdbsum/6uls PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6uls ProSAT]</span></td></tr>
	</table>		</table>
	__TOC__		__TOC__

OCA at 06:21, 19 August 2020

2020-08-19T06:21:04Z

←Older revision		Revision as of 06:21, 19 August 2020
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6uls ~~is ON HOLD until Paper Publication~~	+	====
-		+	<StructureSection load='6uls' size='340' side='right'caption='[[6uls]]' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br>
-	~~Description~~:	+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6uls FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uls OCA], [http://pdbe.org/6uls PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6uls RCSB], [http://www.ebi.ac.uk/pdbsum/6uls PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6uls ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	</table>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Z-disk]]

OCA at 13:24, 29 January 2020

2020-01-29T13:24:49Z

←Older revision		Revision as of 13:24, 29 January 2020
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6uls is ON HOLD	+	The entry 6uls is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "6uls" [edit=sysop:move=sysop]

2019-10-16T04:39:47Z

Protected "6uls" [edit=sysop:move=sysop]

←Older revision

Revision as of 04:39, 16 October 2019

OCA: New page: '''Unreleased structure''' The entry 6uls is ON HOLD Authors: Description: Category: Unreleased Structures

2019-10-16T04:39:46Z

New page: '''Unreleased structure''' The entry 6uls is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 6uls is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]