4gne - Revision history

OCA at 08:51, 20 March 2024

OCA — Wed, 20 Mar 2024 08:51:20 GMT

←Older revision		Revision as of 08:51, 20 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4gne]] 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=4GNE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GNE FirstGlance]. <br>		<table><tr><td colspan='2'>[[4gne]] 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=4GNE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GNE FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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">X-ray diffraction, [[Resolution\|Resolution]] 1.47Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=4gne FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gne OCA], [https://pdbe.org/4gne PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gne RCSB], [https://www.ebi.ac.uk/pdbsum/4gne PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gne 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=4gne FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gne OCA], [https://pdbe.org/4gne PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gne RCSB], [https://www.ebi.ac.uk/pdbsum/4gne PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gne ProSAT]</span></td></tr>
	</table>		</table>
Line 11:		Line 12:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/NSD3_HUMAN NSD3_HUMAN] Histone methyltransferase. Preferentially methylates 'Lys-4' and 'Lys-27' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation, while 'Lys-27' is a mark for transcriptional repression.<ref>PMID:16682010</ref>		[https://www.uniprot.org/uniprot/NSD3_HUMAN NSD3_HUMAN] Histone methyltransferase. Preferentially methylates 'Lys-4' and 'Lys-27' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation, while 'Lys-27' is a mark for transcriptional repression.<ref>PMID:16682010</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The NSD (nuclear receptor SET domain-containing) family members, consisting of NSD1, NSD2 (MMSET/WHSC1), and NSD3 (WHSC1L1), are SET domain-containing methyltransferases and aberrant expression of each member has been implicated in multiple diseases. They have specific mono- and dimethylase activities for H3K36, whereas play nonredundant roles during development. Aside from the well characterized catalytic SET domain, NSD proteins have multiple potential chromatin-binding motifs that are clinically relevant, including the fifth plant homeodomain (PHD5) and the adjacent Cys-His-rich domain (C5HCH) located at the C terminus. Herein, we report the crystal structures of the PHD5-C5HCH module of NSD3, in the free state and in complex with H3(1-7) (H3 residues 1-7), H3(1-15) (H3 residues 1-15), and H3(1-15)K9me3 (H3 residues 1-15 with trimethylation on K9) peptides. These structures reveal that the PHD5 and C5HCH domains fold into a novel integrated PHD-PHD-like structural module with H3 peptide bound only on the surface of PHD5 and provide the molecular basis for the recognition of unmodified H3K4 and trimethylated H3K9 by NSD3 PHD5. Structural studies and binding assays show that differences exist in histone binding specificity of the PHD5 domain between three members of the NSD family. For NSD2, the PHD5-C5HCH:H3 N terminus interaction is largely conserved, although with a stronger preference for unmethylated H3K9 (H3K9me0) than trimethylated H3K9 (H3K9me3), and NSD1 PHD5-C5HCH does not bind to H3 peptides. Our results shed light on how NSD proteins that mediate H3K36 methylation are localized to specific genomic sites and provide implications for the mechanism of functional diversity of NSD proteins.
-
-	The methyltransferase NSD3 has chromatin-binding motifs, PHD5-C5HCH, that are distinct from other NSD (nuclear receptor SET domain) family members in their histone H3 recognition.,He C, Li F, Zhang J, Wu J, Shi Y J Biol Chem. 2013 Feb 15;288(7):4692-703. doi: 10.1074/jbc.M112.426148. Epub 2012, Dec 26. PMID:23269674<ref>PMID:23269674</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4gne" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 07:07, 26 October 2022

OCA — Wed, 26 Oct 2022 07:07:04 GMT

←Older revision		Revision as of 07:07, 26 October 2022
Line 1:		Line 1:

	==Crystal Structure of NSD3 tandem PHD5-C5HCH domains complexed with H3 peptide 1-7==		==Crystal Structure of NSD3 tandem PHD5-C5HCH domains complexed with H3 peptide 1-7==
-	<StructureSection load='4gne' size='340' side='right' caption='[[4gne]], [[Resolution\|resolution]] 1.47Å' scene=''>	+	<StructureSection load='4gne' size='340' side='right'caption='[[4gne]], [[Resolution\|resolution]] 1.47Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4gne]] 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=4GNE OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4GNE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4gne]] 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=4GNE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GNE FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4gnd\|4gnd]], [[4gnf\|4gnf]], [[4gng\|4gng]]</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=4gne FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gne OCA], [https://pdbe.org/4gne PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gne RCSB], [https://www.ebi.ac.uk/pdbsum/4gne PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gne ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">WHSC1L1, NSD3, DC28 ([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-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </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=4gne FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gne OCA], [~~http~~://pdbe.org/4gne PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4gne RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4gne PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4gne ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/NSD3_HUMAN NSD3_HUMAN]] Note=Defects in WHSC1L1 may be involved in non small cell lung carcinomas (NSCLC). Amplified or overexpressed in NSCLC.<ref>PMID:15983384</ref> Note=A chromosomal aberration involving WHSC1L1 is found in childhood acute myeloid leukemia. Translocation t(8;11)(p11.2;p15) with NUP98.	+	[https://www.uniprot.org/uniprot/NSD3_HUMAN NSD3_HUMAN] Note=Defects in WHSC1L1 may be involved in non small cell lung carcinomas (NSCLC). Amplified or overexpressed in NSCLC.<ref>PMID:15983384</ref> Note=A chromosomal aberration involving WHSC1L1 is found in childhood acute myeloid leukemia. Translocation t(8;11)(p11.2;p15) with NUP98.
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/NSD3_HUMAN NSD3_HUMAN]] Histone methyltransferase. Preferentially methylates 'Lys-4' and 'Lys-27' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation, while 'Lys-27' is a mark for transcriptional repression.<ref>PMID:16682010</ref>	+	[https://www.uniprot.org/uniprot/NSD3_HUMAN NSD3_HUMAN] Histone methyltransferase. Preferentially methylates 'Lys-4' and 'Lys-27' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation, while 'Lys-27' is a mark for transcriptional repression.<ref>PMID:16682010</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 22:

	==See Also==		==See Also==
-	*[[Histone methyltransferase\|Histone methyltransferase]]	+	*[[Histone methyltransferase 3D structures\|Histone methyltransferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Histone-lysine N-methyltransferase~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Human~~]]	+	[[Category: Large Structures]]
-	[[Category: He, C]]	+	[[Category: He C]]
-	[[Category: Li, F]]	+	[[Category: Li F]]
-	[[Category: Shi, Y]]	+	[[Category: Shi Y]]
-	[[Category: Wu, J]]	+	[[Category: Wu J]]
-	~~[[Category: Histone]]~~	+
-	~~[[Category: Nuclear protein]]~~	+
-	~~[[Category: Transcription]]~~	+
-	~~[[Category: Transferase-nuclear protein complex]]~~	+
-	~~[[Category: Zinc finger~~]]	+

OCA at 09:34, 11 August 2016

OCA — Thu, 11 Aug 2016 09:34:20 GMT

←Older revision		Revision as of 09:34, 11 August 2016
Line 1:		Line 1:
		+
	==Crystal Structure of NSD3 tandem PHD5-C5HCH domains complexed with H3 peptide 1-7==		==Crystal Structure of NSD3 tandem PHD5-C5HCH domains complexed with H3 peptide 1-7==
	<StructureSection load='4gne' size='340' side='right' caption='[[4gne]], [[Resolution\|resolution]] 1.47Å' scene=''>		<StructureSection load='4gne' size='340' side='right' caption='[[4gne]], [[Resolution\|resolution]] 1.47Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4gne]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GNE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GNE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4gne]] 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=4GNE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GNE FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4gnd\|4gnd]], [[4gnf\|4gnf]], [[4gng\|4gng]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4gnd\|4gnd]], [[4gnf\|4gnf]], [[4gng\|4gng]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">WHSC1L1, NSD3, DC28 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">WHSC1L1, NSD3, DC28 ([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-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </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-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </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=4gne FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gne OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gne RCSB], [http://www.ebi.ac.uk/pdbsum/4gne PDBsum]</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=4gne FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gne OCA], [http://pdbe.org/4gne PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gne RCSB], [http://www.ebi.ac.uk/pdbsum/4gne PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gne ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 21:		Line 22:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4gne" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 29:		Line 31:
	</StructureSection>		</StructureSection>
	[[Category: Histone-lysine N-methyltransferase]]		[[Category: Histone-lysine N-methyltransferase]]
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: He, C]]		[[Category: He, C]]
	[[Category: Li, F]]		[[Category: Li, F]]

OCA at 10:40, 20 January 2015

OCA — Tue, 20 Jan 2015 10:40:07 GMT

←Older revision		Revision as of 10:40, 20 January 2015
Line 1:		Line 1:
-	~~{{STRUCTURE_4gne\| PDB=4gne \| SCENE= }}~~	+	==Crystal Structure of NSD3 tandem PHD5-C5HCH domains complexed with H3 peptide 1-7==
-	===Crystal Structure of NSD3 tandem PHD5-C5HCH domains complexed with H3 peptide 1-7===	+	<StructureSection load='4gne' size='340' side='right' caption='[[4gne]], [[Resolution\|resolution]] 1.47Å' scene=''>
-	~~{{ABSTRACT_PUBMED_23269674}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4gne]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GNE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GNE FirstGlance]. <br>
-	==Disease==	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4gnd\|4gnd]], [[4gnf\|4gnf]], [[4gng\|4gng]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">WHSC1L1, NSD3, DC28 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </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=4gne FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gne OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gne RCSB], [http://www.ebi.ac.uk/pdbsum/4gne PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
	[[http://www.uniprot.org/uniprot/NSD3_HUMAN NSD3_HUMAN]] Note=Defects in WHSC1L1 may be involved in non small cell lung carcinomas (NSCLC). Amplified or overexpressed in NSCLC.<ref>PMID:15983384</ref> Note=A chromosomal aberration involving WHSC1L1 is found in childhood acute myeloid leukemia. Translocation t(8;11)(p11.2;p15) with NUP98.		[[http://www.uniprot.org/uniprot/NSD3_HUMAN NSD3_HUMAN]] Note=Defects in WHSC1L1 may be involved in non small cell lung carcinomas (NSCLC). Amplified or overexpressed in NSCLC.<ref>PMID:15983384</ref> Note=A chromosomal aberration involving WHSC1L1 is found in childhood acute myeloid leukemia. Translocation t(8;11)(p11.2;p15) with NUP98.
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/NSD3_HUMAN NSD3_HUMAN]] Histone methyltransferase. Preferentially methylates 'Lys-4' and 'Lys-27' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation, while 'Lys-27' is a mark for transcriptional repression.<ref>PMID:16682010</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The NSD (nuclear receptor SET domain-containing) family members, consisting of NSD1, NSD2 (MMSET/WHSC1), and NSD3 (WHSC1L1), are SET domain-containing methyltransferases and aberrant expression of each member has been implicated in multiple diseases. They have specific mono- and dimethylase activities for H3K36, whereas play nonredundant roles during development. Aside from the well characterized catalytic SET domain, NSD proteins have multiple potential chromatin-binding motifs that are clinically relevant, including the fifth plant homeodomain (PHD5) and the adjacent Cys-His-rich domain (C5HCH) located at the C terminus. Herein, we report the crystal structures of the PHD5-C5HCH module of NSD3, in the free state and in complex with H3(1-7) (H3 residues 1-7), H3(1-15) (H3 residues 1-15), and H3(1-15)K9me3 (H3 residues 1-15 with trimethylation on K9) peptides. These structures reveal that the PHD5 and C5HCH domains fold into a novel integrated PHD-PHD-like structural module with H3 peptide bound only on the surface of PHD5 and provide the molecular basis for the recognition of unmodified H3K4 and trimethylated H3K9 by NSD3 PHD5. Structural studies and binding assays show that differences exist in histone binding specificity of the PHD5 domain between three members of the NSD family. For NSD2, the PHD5-C5HCH:H3 N terminus interaction is largely conserved, although with a stronger preference for unmethylated H3K9 (H3K9me0) than trimethylated H3K9 (H3K9me3), and NSD1 PHD5-C5HCH does not bind to H3 peptides. Our results shed light on how NSD proteins that mediate H3K36 methylation are localized to specific genomic sites and provide implications for the mechanism of functional diversity of NSD proteins.

-	~~==Function==~~	+	The methyltransferase NSD3 has chromatin-binding motifs, PHD5-C5HCH, that are distinct from other NSD (nuclear receptor SET domain) family members in their histone H3 recognition.,He C, Li F, Zhang J, Wu J, Shi Y J Biol Chem. 2013 Feb 15;288(7):4692-703. doi: 10.1074/jbc.M112.426148. Epub 2012, Dec 26. PMID:23269674<ref>PMID:23269674</ref>
-	~~[[http://www.uniprot.org/uniprot/NSD3_HUMAN NSD3_HUMAN]] Histone~~ methyltransferase~~. Preferentially methylates 'Lys~~-~~4' and 'Lys~~-~~27' of~~ histone H3. ~~H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation~~, ~~while 'Lys~~-~~27' is a mark for transcriptional repression~~.<ref>PMID:~~16682010~~</ref>	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[4gne]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Homo_sapiens Homo sapiens]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=4GNE OCA].~~	+	</div>

-	==~~Reference~~==	+	==See Also==
-	~~<ref group~~=~~"xtra">PMID:023269674</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	*[[Histone methyltransferase\|Histone methyltransferase]]
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Histone-lysine N-methyltransferase]]		[[Category: Histone-lysine N-methyltransferase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: He, C.]]	+	[[Category: He, C]]
-	[[Category: Li, F.]]	+	[[Category: Li, F]]
-	[[Category: Shi, Y.]]	+	[[Category: Shi, Y]]
-	[[Category: Wu, J.]]	+	[[Category: Wu, J]]
	[[Category: Histone]]		[[Category: Histone]]
	[[Category: Nuclear protein]]		[[Category: Nuclear protein]]

OCA at 08:52, 4 September 2013

OCA — Wed, 04 Sep 2013 08:52:31 GMT

←Older revision		Revision as of 08:52, 4 September 2013
Line 1:		Line 1:
	{{STRUCTURE_4gne\| PDB=4gne \| SCENE= }}		{{STRUCTURE_4gne\| PDB=4gne \| SCENE= }}
	===Crystal Structure of NSD3 tandem PHD5-C5HCH domains complexed with H3 peptide 1-7===		===Crystal Structure of NSD3 tandem PHD5-C5HCH domains complexed with H3 peptide 1-7===
		+	{{ABSTRACT_PUBMED_23269674}}

	==Disease==		==Disease==
-	[[http://www.uniprot.org/uniprot/NSD3_HUMAN NSD3_HUMAN]] Note=Defects in WHSC1L1 may be involved in non small cell lung carcinomas (NSCLC). Amplified or overexpressed in NSCLC.<ref>PMID:15983384</ref> Note=A chromosomal aberration involving WHSC1L1 is found in childhood acute myeloid leukemia. Translocation t(8;11)(p11.2;p15) with NUP98.	+	[[http://www.uniprot.org/uniprot/NSD3_HUMAN NSD3_HUMAN]] Note=Defects in WHSC1L1 may be involved in non small cell lung carcinomas (NSCLC). Amplified or overexpressed in NSCLC.<ref>PMID:15983384</ref> Note=A chromosomal aberration involving WHSC1L1 is found in childhood acute myeloid leukemia. Translocation t(8;11)(p11.2;p15) with NUP98.

	==Function==		==Function==
-	[[http://www.uniprot.org/uniprot/NSD3_HUMAN NSD3_HUMAN]] Histone methyltransferase. Preferentially methylates 'Lys-4' and 'Lys-27' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation, while 'Lys-27' is a mark for transcriptional repression.<ref>PMID:16682010</ref>	+	[[http://www.uniprot.org/uniprot/NSD3_HUMAN NSD3_HUMAN]] Histone methyltransferase. Preferentially methylates 'Lys-4' and 'Lys-27' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation, while 'Lys-27' is a mark for transcriptional repression.<ref>PMID:16682010</ref>

	==About this Structure==		==About this Structure==
Line 12:		Line 13:

	==Reference==		==Reference==
-	<references group="xtra"/><references/>	+	<ref group="xtra">PMID:023269674</ref><references group="xtra"/><references/>
	[[Category: Histone-lysine N-methyltransferase]]		[[Category: Histone-lysine N-methyltransferase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA at 16:34, 24 March 2013

OCA — Sun, 24 Mar 2013 16:34:36 GMT

←Older revision		Revision as of 16:34, 24 March 2013
Line 1:		Line 1:
-	[[Image:4gne.jpg\|left\|200px]]
-
	{{STRUCTURE_4gne\| PDB=4gne \| SCENE= }}		{{STRUCTURE_4gne\| PDB=4gne \| SCENE= }}
-
	===Crystal Structure of NSD3 tandem PHD5-C5HCH domains complexed with H3 peptide 1-7===		===Crystal Structure of NSD3 tandem PHD5-C5HCH domains complexed with H3 peptide 1-7===

		+	==Disease==
		+	[[http://www.uniprot.org/uniprot/NSD3_HUMAN NSD3_HUMAN]] Note=Defects in WHSC1L1 may be involved in non small cell lung carcinomas (NSCLC). Amplified or overexpressed in NSCLC.<ref>PMID:15983384</ref> Note=A chromosomal aberration involving WHSC1L1 is found in childhood acute myeloid leukemia. Translocation t(8;11)(p11.2;p15) with NUP98.
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/NSD3_HUMAN NSD3_HUMAN]] Histone methyltransferase. Preferentially methylates 'Lys-4' and 'Lys-27' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation, while 'Lys-27' is a mark for transcriptional repression.<ref>PMID:16682010</ref>

	==About this Structure==		==About this Structure==
	[[4gne]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GNE OCA].		[[4gne]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GNE OCA].
		+
		+	==Reference==
		+	<references group="xtra"/><references/>
	[[Category: Histone-lysine N-methyltransferase]]		[[Category: Histone-lysine N-methyltransferase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA at 09:36, 2 January 2013

OCA — Wed, 02 Jan 2013 09:36:55 GMT

←Older revision		Revision as of 09:36, 2 January 2013
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:4gne.jpg\|left\|200px]]

-	~~The entry~~ 4gne ~~is ON HOLD~~ ~~until Paper Publication~~	+	{{STRUCTURE_4gne\| PDB=4gne \| SCENE= }}

-	~~Authors: Li, F., He, C., Wu, J., Shi, Y.~~	+	===Crystal Structure of NSD3 tandem PHD5-C5HCH domains complexed with H3 peptide 1-7===

-	~~Description: Crystal~~ Structure ~~of NSD3 tandem PHD5-C5HCH domains complexed~~ with ~~H3 peptide 1~~-7	+
		+	==About this Structure==
		+	[[4gne]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GNE OCA].
		+	[[Category: Histone-lysine N-methyltransferase]]
		+	[[Category: Homo sapiens]]
		+	[[Category: He, C.]]
		+	[[Category: Li, F.]]
		+	[[Category: Shi, Y.]]
		+	[[Category: Wu, J.]]
		+	[[Category: Histone]]
		+	[[Category: Nuclear protein]]
		+	[[Category: Transcription]]
		+	[[Category: Transferase-nuclear protein complex]]
		+	[[Category: Zinc finger]]

OCA at 04:51, 12 September 2012

OCA — Wed, 12 Sep 2012 04:51:49 GMT

←Older revision		Revision as of 04:51, 12 September 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4gne is ON HOLD	+	The entry 4gne is ON HOLD until Paper Publication

	Authors: Li, F., He, C., Wu, J., Shi, Y.		Authors: Li, F., He, C., Wu, J., Shi, Y.

	Description: Crystal Structure of NSD3 tandem PHD5-C5HCH domains complexed with H3 peptide 1-7		Description: Crystal Structure of NSD3 tandem PHD5-C5HCH domains complexed with H3 peptide 1-7

OCA at 04:55, 5 September 2012

OCA — Wed, 05 Sep 2012 04:55:10 GMT

←Older revision		Revision as of 04:55, 5 September 2012
Line 3:		Line 3:
	The entry 4gne is ON HOLD		The entry 4gne is ON HOLD

-	Authors: Li, F., He, C., Wu, J, Shi, Y	+	Authors: Li, F., He, C., Wu, J., Shi, Y.

	Description: Crystal Structure of NSD3 tandem PHD5-C5HCH domains complexed with H3 peptide 1-7		Description: Crystal Structure of NSD3 tandem PHD5-C5HCH domains complexed with H3 peptide 1-7

OCA: Protected "4gne" [edit=sysop:move=sysop]

OCA — Wed, 22 Aug 2012 05:38:48 GMT

Protected "4gne" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:38, 22 August 2012