5fe1 - Revision history

OCA at 06:47, 19 July 2023

OCA — Wed, 19 Jul 2023 06:47:50 GMT

←Older revision		Revision as of 06:47, 19 July 2023
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	<StructureSection load='5fe1' size='340' side='right'caption='[[5fe1]], [[Resolution\|resolution]] 2.22Å' scene=''>		<StructureSection load='5fe1' size='340' side='right'caption='[[5fe1]], [[Resolution\|resolution]] 2.22Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5fe1]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FE1 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5FE1 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5fe1]] 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=5FE1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FE1 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=12Q:1~~-~~METHYLQUINOLIN-2(1H)-ONE'>12Q</scene>, <scene name='pdbligand=EDO:1~~,2~~-ETHANEDIOL'>EDO</scene>~~</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]] 2.22Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>KAT2B, PCAF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~9606 HUMAN])</td~~><~~/tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=12Q:1-METHYLQUINOLIN-2(1H)-ONE'>12Q</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks'>[http~~:~~//en.wikipedia.org/wiki/Histone_acetyltransferase Histone acetyltransferase]~~, ~~with EC number [http://www.brenda~~-~~enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48]~~ </~~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=5fe1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fe1 OCA], [https://pdbe.org/5fe1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fe1 RCSB], [https://www.ebi.ac.uk/pdbsum/5fe1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fe1 ProSAT]</span></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=5fe1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fe1 OCA], [~~http~~://pdbe.org/5fe1 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5fe1 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5fe1 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5fe1 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/KAT2B_HUMAN KAT2B_HUMAN]] Functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Has significant histone acetyltransferase activity with core histones (H3 and H4), and also with nucleosome core particles. Also acetylates non-histone proteins, such as ACLY. Inhibits cell-cycle progression and counteracts the mitogenic activity of the adenoviral oncoprotein E1A. 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.<ref>PMID:8684459</ref> <ref>PMID:9707565</ref> <ref>PMID:10675335</ref> <ref>PMID:23932781</ref>	+	[https://www.uniprot.org/uniprot/KAT2B_HUMAN KAT2B_HUMAN] Functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Has significant histone acetyltransferase activity with core histones (H3 and H4), and also with nucleosome core particles. Also acetylates non-histone proteins, such as ACLY. Inhibits cell-cycle progression and counteracts the mitogenic activity of the adenoviral oncoprotein E1A. 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.<ref>PMID:8684459</ref> <ref>PMID:9707565</ref> <ref>PMID:10675335</ref> <ref>PMID:23932781</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Histone acetyltransferase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Arrowsmith~~, C H~~]]	+	[[Category: Arrowsmith CH]]
-	[[Category: Bountra, C]]	+	[[Category: Bountra C]]
-	[[Category: Chaikuad, A]]	+	[[Category: Chaikuad A]]
-	~~[[Category: Delft, F von~~]]	+	[[Category: Edwards AM]]
-	[[Category: Edwards~~, A M~~]]	+	[[Category: Knapp S]]
-	[[Category: Knapp, S]]	+	[[Category: Von Delft F]]
-	[[Category: ~~Structural genomic]]~~	+
-	~~[[Category: Acetylation]]~~	+
-	~~[[Category: Acetyllysine]]~~	+
-	~~[[Category: Bromodomain]]~~	+
-	~~[[Category: Epigenetic]]~~	+
-	~~[[Category: Histone]]~~	+
-	~~[[Category: Histone acetyltransferase kat2b]]~~	+
-	~~[[Category: Signaling protein~~]]	+

OCA at 07:14, 6 May 2020

OCA — Wed, 06 May 2020 07:14:03 GMT

←Older revision		Revision as of 07:14, 6 May 2020
Line 1:		Line 1:

	==Crystal structure of human PCAF bromodomain in complex with fragment BR004 (fragment 1)==		==Crystal structure of human PCAF bromodomain in complex with fragment BR004 (fragment 1)==
-	<StructureSection load='5fe1' size='340' side='right' caption='[[5fe1]], [[Resolution\|resolution]] 2.22Å' scene=''>	+	<StructureSection load='5fe1' size='340' side='right'caption='[[5fe1]], [[Resolution\|resolution]] 2.22Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5fe1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FE1 OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5FE1 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5fe1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FE1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FE1 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=12Q:1-METHYLQUINOLIN-2(1H)-ONE'>12Q</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=12Q:1-METHYLQUINOLIN-2(1H)-ONE'>12Q</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">KAT2B, PCAF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone_acetyltransferase Histone acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone_acetyltransferase Histone acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5fe1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fe1 OCA], [http://pdbe.org/5fe1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fe1 RCSB], [http://www.ebi.ac.uk/pdbsum/5fe1 PDBsum]</span></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=5fe1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fe1 OCA], [http://pdbe.org/5fe1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fe1 RCSB], [http://www.ebi.ac.uk/pdbsum/5fe1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fe1 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	</div>		</div>
	<div class="pdbe-citations 5fe1" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5fe1" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Histone acetyltransferase 3D structures\|Histone acetyltransferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 24:		Line 28:
	</StructureSection>		</StructureSection>
	[[Category: Histone acetyltransferase]]		[[Category: Histone acetyltransferase]]
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Arrowsmith, C H]]		[[Category: Arrowsmith, C H]]
	[[Category: Bountra, C]]		[[Category: Bountra, C]]

OCA at 16:31, 10 May 2016

OCA — Tue, 10 May 2016 16:31:24 GMT

←Older revision		Revision as of 16:31, 10 May 2016
Line 1:		Line 1:
		+
	==Crystal structure of human PCAF bromodomain in complex with fragment BR004 (fragment 1)==		==Crystal structure of human PCAF bromodomain in complex with fragment BR004 (fragment 1)==
	<StructureSection load='5fe1' size='340' side='right' caption='[[5fe1]], [[Resolution\|resolution]] 2.22Å' scene=''>		<StructureSection load='5fe1' size='340' side='right' caption='[[5fe1]], [[Resolution\|resolution]] 2.22Å' scene=''>
Line 9:		Line 10:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/KAT2B_HUMAN KAT2B_HUMAN]] Functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Has significant histone acetyltransferase activity with core histones (H3 and H4), and also with nucleosome core particles. Also acetylates non-histone proteins, such as ACLY. Inhibits cell-cycle progression and counteracts the mitogenic activity of the adenoviral oncoprotein E1A. 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.<ref>PMID:8684459</ref> <ref>PMID:9707565</ref> <ref>PMID:10675335</ref> <ref>PMID:23932781</ref>		[[http://www.uniprot.org/uniprot/KAT2B_HUMAN KAT2B_HUMAN]] Functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Has significant histone acetyltransferase activity with core histones (H3 and H4), and also with nucleosome core particles. Also acetylates non-histone proteins, such as ACLY. Inhibits cell-cycle progression and counteracts the mitogenic activity of the adenoviral oncoprotein E1A. 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.<ref>PMID:8684459</ref> <ref>PMID:9707565</ref> <ref>PMID:10675335</ref> <ref>PMID:23932781</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The P300/CBP-associated factor plays a central role in retroviral infection and cancer development, and the C-terminal bromodomain provides an opportunity for selective targeting. Here, we report several new classes of acetyl-lysine mimetic ligands ranging from mM to low micromolar affinity that were identified using fragment screening approaches. The binding modes of the most attractive fragments were determined using high resolution crystal structures providing chemical starting points and structural models for the development of potent and selective PCAF inhibitors.
		+
		+	Structure-Based Identification of Inhibitory Fragments Targeting the p300/CBP-Associated Factor Bromodomain.,Chaikuad A, Lang S, Brennan PE, Temperini C, Fedorov O, Hollander J, Nachane R, Abell C, Muller S, Siegal G, Knapp S J Med Chem. 2016 Feb 25;59(4):1648-53. doi: 10.1021/acs.jmedchem.5b01719. Epub, 2016 Jan 13. PMID:26731131<ref>PMID:26731131</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5fe1" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 20:36, 13 January 2016

OCA — Wed, 13 Jan 2016 20:36:21 GMT

←Older revision		Revision as of 20:36, 13 January 2016
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==Crystal structure of human PCAF bromodomain in complex with fragment BR004 (fragment 1)==
-		+	<StructureSection load='5fe1' size='340' side='right' caption='[[5fe1]], [[Resolution\|resolution]] 2.22Å' scene=''>
-	~~The entry~~ 5fe1 is ~~ON HOLD~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5fe1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FE1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FE1 FirstGlance]. <br>
-	~~Authors~~: ~~Chaikuad, A~~.~~, von Delft, F~~., ~~Bountra~~, C., ~~Arrowsmith, C~~.H., ~~Edwards, A~~.M., ~~Knapp~~, S., ~~Structural Genomics Consortium (SGC)~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=12Q:1-METHYLQUINOLIN-2(1H)-ONE'>12Q</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
-		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone_acetyltransferase Histone acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48] </span></td></tr>
-	~~Description~~: ~~Crystal structure of human PCAF bromodomain in complex~~ with ~~fragment BR004~~ (~~FR1~~)	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5fe1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fe1 OCA], [http://pdbe.org/5fe1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fe1 RCSB], [http://www.ebi.ac.uk/pdbsum/5fe1 PDBsum]</span></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/KAT2B_HUMAN KAT2B_HUMAN]] Functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Has significant histone acetyltransferase activity with core histones (H3 and H4), and also with nucleosome core particles. Also acetylates non-histone proteins, such as ACLY. Inhibits cell-cycle progression and counteracts the mitogenic activity of the adenoviral oncoprotein E1A. 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.<ref>PMID:8684459</ref> <ref>PMID:9707565</ref> <ref>PMID:10675335</ref> <ref>PMID:23932781</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Histone acetyltransferase]]
		+	[[Category: Arrowsmith, C H]]
		+	[[Category: Bountra, C]]
	[[Category: Chaikuad, A]]		[[Category: Chaikuad, A]]
		+	[[Category: Delft, F von]]
		+	[[Category: Edwards, A M]]
	[[Category: Knapp, S]]		[[Category: Knapp, S]]
-	[[Category: ~~Bountra, C~~]]	+	[[Category: Structural genomic]]
-	[[Category: ~~Arrowsmith, C.H~~]]	+	[[Category: Acetylation]]
-	[[Category: ~~Von Delft, F~~]]	+	[[Category: Acetyllysine]]
-	[[Category: ~~Edwards, A.M~~]]	+	[[Category: Bromodomain]]
-	[[Category: ~~Structural Genomics Consortium (Sgc)~~]]	+	[[Category: Epigenetic]]
		+	[[Category: Histone]]
		+	[[Category: Histone acetyltransferase kat2b]]
		+	[[Category: Signaling protein]]

OCA: Protected "5fe1" [edit=sysop:move=sysop]

OCA — Wed, 23 Dec 2015 11:32:12 GMT

Protected "5fe1" [edit=sysop:move=sysop]

←Older revision

Revision as of 11:32, 23 December 2015

OCA: New page: '''Unreleased structure''' The entry 5fe1 is ON HOLD Authors: Chaikuad, A., von Delft, F., Bountra, C., Arrowsmith, C.H., Edwards, A.M., Knapp, S., Structural Genomics Consortium (SGC) ...

OCA — Wed, 23 Dec 2015 11:32:11 GMT

New page: '''Unreleased structure''' The entry 5fe1 is ON HOLD Authors: Chaikuad, A., von Delft, F., Bountra, C., Arrowsmith, C.H., Edwards, A.M., Knapp, S., Structural Genomics Consortium (SGC) ...

New page

'''Unreleased structure'''

The entry 5fe1 is ON HOLD

Authors: Chaikuad, A., von Delft, F., Bountra, C., Arrowsmith, C.H., Edwards, A.M., Knapp, S., Structural Genomics Consortium (SGC)

Description: Crystal structure of human PCAF bromodomain in complex with fragment BR004 (FR1)
[[Category: Unreleased Structures]]
[[Category: Chaikuad, A]]
[[Category: Knapp, S]]
[[Category: Bountra, C]]
[[Category: Arrowsmith, C.H]]
[[Category: Von Delft, F]]
[[Category: Edwards, A.M]]
[[Category: Structural Genomics Consortium (Sgc)]]