8bpc - Revision history

OCA at 06:49, 24 July 2024

2024-07-24T06:49:00Z

← Older revision		Revision as of 06:49, 24 July 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[8bpc]] is a 3 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=8BPC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BPC FirstGlance]. <br>		<table><tr><td colspan='2'>[[8bpc]] is a 3 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=8BPC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BPC FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SHH:OCTANEDIOIC+ACID+HYDROXYAMIDE+PHENYLAMIDE'>SHH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution\|Resolution]] 2.8Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SHH:OCTANEDIOIC+ACID+HYDROXYAMIDE+PHENYLAMIDE'>SHH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=8bpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bpc OCA], [https://pdbe.org/8bpc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bpc RCSB], [https://www.ebi.ac.uk/pdbsum/8bpc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bpc 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=8bpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bpc OCA], [https://pdbe.org/8bpc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bpc RCSB], [https://www.ebi.ac.uk/pdbsum/8bpc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bpc ProSAT]</span></td></tr>
	</table>		</table>
	~~== Disease ==~~
	~~[https://www.uniprot.org/uniprot/SIN3B_HUMAN SIN3B_HUMAN] SIN3A-related intellectual disability syndrome due to a point mutation.~~
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/~~SIN3B_HUMAN SIN3B_HUMAN~~] ~~Acts as~~ a transcriptional repressor. Interacts with ~~MXI1 to repress MYC responsive~~ genes and ~~antagonize MYC oncogenic activities~~. ~~Interacts~~ with ~~MAD~~-~~MAX heterodimers~~ by ~~binding~~ to ~~MAD~~. ~~The heterodimer then represses transcription~~ by ~~tethering~~ SIN3B ~~to DNA~~. ~~Also forms~~ a ~~complex with FOXK1 which represses transcription~~. ~~With FOXK1, regulates cell cycle progression probably by repressing cell cycle inhibitor genes expression~~.[~~UniProtKB:Q62141~~]		[https://www.uniprot.org/uniprot/HDAC2_HUMAN HDAC2_HUMAN] Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR. Interacts in the late S-phase of DNA-replication with DNMT1 in the other transcriptional repressor complex composed of DNMT1, DMAP1, PCNA, CAF1. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development.<ref>PMID:19343227</ref>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Lysine acetylation in histone tails is a key post-translational modification that controls transcription activation. Histone deacetylase complexes remove histone acetylation, thereby repressing transcription and regulating the transcriptional output of each gene. Although these complexes are drug targets and crucial regulators of organismal physiology, their structure and mechanisms of action are largely unclear. Here, we present the structure of a complete human SIN3B histone deacetylase holo-complex with and without a substrate mimic. Remarkably, SIN3B encircles the deacetylase and contacts its allosteric basic patch thereby stimulating catalysis. A SIN3B loop inserts into the catalytic tunnel, rearranges to accommodate the acetyl-lysine moiety, and stabilises the substrate for specific deacetylation, which is guided by a substrate receptor subunit. Our findings provide a model of specificity for a main transcriptional regulator conserved from yeast to human and a resource of protein-protein interactions for future drug designs.

			Mechanism of assembly, activation and lysine selection by the SIN3B histone deacetylase complex.,Wan MSM, Muhammad R, Koliopoulos MG, Roumeliotis TI, Choudhary JS, Alfieri C Nat Commun. 2023 May 3;14(1):2556. doi: 10.1038/s41467-023-38276-0. PMID:37137925<ref>PMID:37137925</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 8bpc" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[Histone deacetylase 3D structures\|Histone deacetylase 3D structures]]
			== References ==
			<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 06:51, 10 May 2023

2023-05-10T06:51:49Z

← Older revision		Revision as of 06:51, 10 May 2023
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	~~'''Unreleased structure'''~~

	~~The entry~~ 8bpc is ~~ON HOLD until Paper Publication~~		==Cryo-EM structure of the human SIN3B histone deacetylase core complex with SAHA at 2.8 Angstrom==
			<StructureSection load='8bpc' size='340' side='right'caption='[[8bpc]], [[Resolution\|resolution]] 2.80Å' scene=''>
	~~Authors~~:		== Structural highlights ==
			<table><tr><td colspan='2'>[[8bpc]] is a 3 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=8BPC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BPC FirstGlance]. <br>
	~~Description~~:		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SHH:OCTANEDIOIC+ACID+HYDROXYAMIDE+PHENYLAMIDE'>SHH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	[[Category: ~~Unreleased~~ Structures]]		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8bpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bpc OCA], [https://pdbe.org/8bpc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bpc RCSB], [https://www.ebi.ac.uk/pdbsum/8bpc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bpc ProSAT]</span></td></tr>
			</table>
			== Disease ==
			[https://www.uniprot.org/uniprot/SIN3B_HUMAN SIN3B_HUMAN] SIN3A-related intellectual disability syndrome due to a point mutation.
			== Function ==
			[https://www.uniprot.org/uniprot/SIN3B_HUMAN SIN3B_HUMAN] Acts as a transcriptional repressor. Interacts with MXI1 to repress MYC responsive genes and antagonize MYC oncogenic activities. Interacts with MAD-MAX heterodimers by binding to MAD. The heterodimer then represses transcription by tethering SIN3B to DNA. Also forms a complex with FOXK1 which represses transcription. With FOXK1, regulates cell cycle progression probably by repressing cell cycle inhibitor genes expression.[UniProtKB:Q62141]
			__TOC__
			</StructureSection>
			[[Category: Homo sapiens]]
			[[Category: Large Structures]]
			[[Category: Alfieri C]]
			[[Category: Koliopolous MG]]
			[[Category: Muhammad R]]
			[[Category: Wan MSM]]

OCA at 07:21, 14 December 2022

2022-12-14T07:21:13Z

← Older revision		Revision as of 07:21, 14 December 2022
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	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 8bpc is ON HOLD		The entry 8bpc is ON HOLD until Paper Publication

	Authors:		Authors:

OCA at 05:11, 7 December 2022

2022-12-07T05:11:42Z

← Older revision		Revision as of 05:11, 7 December 2022
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	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 8bpc is ON HOLD ~~until sometime in the future~~		The entry 8bpc is ON HOLD

	Authors:		Authors:

OCA at 08:22, 30 November 2022

2022-11-30T08:22:46Z

← Older revision		Revision as of 08:22, 30 November 2022
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	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 8bpc is ON HOLD		The entry 8bpc is ON HOLD until sometime in the future

	Authors:		Authors:

OCA: Protected "8bpc" [edit=sysop:move=sysop]

2022-11-24T08:05:23Z

Protected "8bpc" [edit=sysop:move=sysop]

← Older revision	Revision as of 08:05, 24 November 2022
(No difference)

OCA: New page: '''Unreleased structure''' The entry 8bpc is ON HOLD Authors: Description: Category: Unreleased Structures

2022-11-24T08:05:22Z

New page: '''Unreleased structure''' The entry 8bpc is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 8bpc is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]