3rib - Revision history

OCA at 08:36, 20 March 2024

OCA — Wed, 20 Mar 2024 08:36:03 GMT

←Older revision		Revision as of 08:36, 20 March 2024
Line 3:		Line 3:
	<StructureSection load='3rib' size='340' side='right'caption='[[3rib]], [[Resolution\|resolution]] 2.79Å' scene=''>		<StructureSection load='3rib' size='340' side='right'caption='[[3rib]], [[Resolution\|resolution]] 2.79Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3rib]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RIB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RIB FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3rib]] 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=3RIB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RIB FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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">X-ray diffraction, [[Resolution\|Resolution]] 2.79Å</td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SMYD2, KMT3C ([https://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=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3rib FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rib OCA], [https://pdbe.org/3rib PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rib RCSB], [https://www.ebi.ac.uk/pdbsum/3rib PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rib 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=3rib FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rib OCA], [https://pdbe.org/3rib PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rib RCSB], [https://www.ebi.ac.uk/pdbsum/3rib PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rib ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/SMYD2_HUMAN SMYD2_HUMAN]] Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins. Specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). Has also methyltransferase activity toward non-histone proteins such as p53/TP53 and RB1. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates 'Lys-860' of RB1/RB.<ref>PMID:17108971</ref> <ref>PMID:17805299</ref> <ref>PMID:18065756</ref> <ref>PMID:20870719</ref>	+	[https://www.uniprot.org/uniprot/SMYD2_HUMAN SMYD2_HUMAN] Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins. Specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). Has also methyltransferase activity toward non-histone proteins such as p53/TP53 and RB1. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates 'Lys-860' of RB1/RB.<ref>PMID:17108971</ref> <ref>PMID:17805299</ref> <ref>PMID:18065756</ref> <ref>PMID:20870719</ref>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	The SET- and myeloid-Nervy-DEAF-1 (MYND)-domain containing (Smyd) lysine methyltransferases 1-3 share relatively high sequence similarity but exhibit divergence in the substrate specificity. Here we report the crystal structure of the full-length human Smyd2 in complex with S-adenosyl-L-homocysteine (AdoHcy). Although the Smyd1-3 enzymes are similar in the overall structure, detailed comparisons demonstrate that they differ substantially in the potential substrate-binding site. The binding site of Smyd3 consists mainly of a deep and narrow pocket, while those of Smyd1 and Smyd2 consist of a comparable pocket and a long groove. In addition, Smyd2, which has lysine methyltransferase activity on histone H3-lysine 36, exhibits substantial differences in the wall of the substrate-binding pocket compared with those of Smyd1 and Smyd3 which have activity specifically on histone H3-lysine 4. The differences in the substrate-binding site might account for the observed divergence in the specificity and methylation state of the substrates. Further modeling study of Smyd2 in complex with a p53 peptide indicates that mono-methylation of p53-Lys(372) might result in steric conflict of the methyl group with the surrounding residues of Smyd2, providing a structural explanation for the inhibitory effect of the SET7/9-mediated mono-methylation of p53-Lys(372) on the Smyd2-mediated methylation of p53-Lys(370).	+
-		+
-	Structure of human lysine methyltransferase Smyd2 reveals insights into the substrate divergence in Smyd proteins.,Xu S, Zhong C, Zhang T, Ding J J Mol Cell Biol. 2011 Jul 1. PMID:21724641<ref>PMID:21724641</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 3rib" style="background-color:#fffaf0;"></div~~>	+

	==See Also==		==See Also==
Line 26:		Line 17:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Ding, J]]	+	[[Category: Ding J]]
-	[[Category: Xu, S]]	+	[[Category: Xu S]]
-	[[Category: Zhang, T]]	+	[[Category: Zhang T]]
-	[[Category: Zhong, C]]	+	[[Category: Zhong C]]
-	~~[[Category: H3k36]]~~	+
-	~~[[Category: H3k4]]~~	+
-	~~[[Category: Histone lysine methyltransferase]]~~	+
-	~~[[Category: Histone methylation]]~~	+
-	~~[[Category: Mynd]]~~	+
-	~~[[Category: Set domain]]~~	+
-	~~[[Category: Smyd protein]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 06:04, 15 June 2022

OCA — Wed, 15 Jun 2022 06:04:52 GMT

←Older revision		Revision as of 06:04, 15 June 2022
Line 1:		Line 1:

	==Human lysine methyltransferase Smyd2 in complex with AdoHcy==		==Human lysine methyltransferase Smyd2 in complex with AdoHcy==
-	<StructureSection load='3rib' size='340' side='right' caption='[[3rib]], [[Resolution\|resolution]] 2.79Å' scene=''>	+	<StructureSection load='3rib' size='340' side='right'caption='[[3rib]], [[Resolution\|resolution]] 2.79Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3rib]] 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=3RIB OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3RIB FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3rib]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RIB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RIB FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <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=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SMYD2, KMT3C ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SMYD2, KMT3C ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3rib FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rib OCA], [~~http~~://pdbe.org/3rib PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3rib RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3rib PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3rib 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=3rib FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rib OCA], [https://pdbe.org/3rib PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rib RCSB], [https://www.ebi.ac.uk/pdbsum/3rib PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rib ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/SMYD2_HUMAN SMYD2_HUMAN]] Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins. Specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). Has also methyltransferase activity toward non-histone proteins such as p53/TP53 and RB1. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates 'Lys-860' of RB1/RB.<ref>PMID:17108971</ref> <ref>PMID:17805299</ref> <ref>PMID:18065756</ref> <ref>PMID:20870719</ref>	+	[[https://www.uniprot.org/uniprot/SMYD2_HUMAN SMYD2_HUMAN]] Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins. Specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). Has also methyltransferase activity toward non-histone proteins such as p53/TP53 and RB1. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates 'Lys-860' of RB1/RB.<ref>PMID:17108971</ref> <ref>PMID:17805299</ref> <ref>PMID:18065756</ref> <ref>PMID:20870719</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 19:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 3rib" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3rib" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Histone methyltransferase 3D structures\|Histone methyltransferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 24:		Line 27:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Ding, J]]		[[Category: Ding, J]]
	[[Category: Xu, S]]		[[Category: Xu, S]]

OCA at 09:26, 8 November 2017

OCA — Wed, 08 Nov 2017 09:26:20 GMT

←Older revision		Revision as of 09:26, 8 November 2017
Line 19:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 3rib" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3rib" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Histone methyltransferase\|Histone methyltransferase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 06:56, 5 August 2016

OCA — Fri, 05 Aug 2016 06:56:01 GMT

←Older revision		Revision as of 06:56, 5 August 2016
Line 1:		Line 1:
		+
	==Human lysine methyltransferase Smyd2 in complex with AdoHcy==		==Human lysine methyltransferase Smyd2 in complex with AdoHcy==
	<StructureSection load='3rib' size='340' side='right' caption='[[3rib]], [[Resolution\|resolution]] 2.79Å' scene=''>		<StructureSection load='3rib' size='340' side='right' caption='[[3rib]], [[Resolution\|resolution]] 2.79Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3rib]] 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=3RIB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RIB FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3rib]] 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=3RIB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RIB FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <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=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SMYD2, KMT3C ([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">SMYD2, KMT3C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3rib FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rib OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rib RCSB], [http://www.ebi.ac.uk/pdbsum/3rib 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=3rib FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rib OCA], [http://pdbe.org/3rib PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3rib RCSB], [http://www.ebi.ac.uk/pdbsum/3rib PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3rib ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	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 3rib" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 24:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Ding, J]]		[[Category: Ding, J]]
	[[Category: Xu, S]]		[[Category: Xu, S]]

OCA at 00:01, 25 December 2014

OCA — Thu, 25 Dec 2014 00:01:39 GMT

←Older revision		Revision as of 00:01, 25 December 2014
Line 7:		Line 7:
	<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=3rib FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rib OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rib RCSB], [http://www.ebi.ac.uk/pdbsum/3rib 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=3rib FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rib OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rib RCSB], [http://www.ebi.ac.uk/pdbsum/3rib PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/SMYD2_HUMAN SMYD2_HUMAN]] Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins. Specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). Has also methyltransferase activity toward non-histone proteins such as p53/TP53 and RB1. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates 'Lys-860' of RB1/RB.<ref>PMID:17108971</ref> <ref>PMID:17805299</ref> <ref>PMID:18065756</ref> <ref>PMID:20870719</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 10:23, 19 December 2014

OCA — Fri, 19 Dec 2014 10:23:06 GMT

←Older revision		Revision as of 10:23, 19 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3rib~~\| ~~PDB~~=3rib \| ~~SCENE~~= }}	+	==Human lysine methyltransferase Smyd2 in complex with AdoHcy==
-	===~~Human~~ lysine ~~methyltransferase~~ Smyd2 in complex with AdoHcy~~===~~	+	<StructureSection load='3rib' size='340' side='right' caption='[[3rib]], [[Resolution\|resolution]] 2.79Å' scene=''>
-	~~{{ABSTRACT_PUBMED_21724641}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3rib]] 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=3RIB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RIB FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SMYD2, KMT3C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3rib FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rib OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rib RCSB], [http://www.ebi.ac.uk/pdbsum/3rib PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The SET- and myeloid-Nervy-DEAF-1 (MYND)-domain containing (Smyd) lysine methyltransferases 1-3 share relatively high sequence similarity but exhibit divergence in the substrate specificity. Here we report the crystal structure of the full-length human Smyd2 in complex with S-adenosyl-L-homocysteine (AdoHcy). Although the Smyd1-3 enzymes are similar in the overall structure, detailed comparisons demonstrate that they differ substantially in the potential substrate-binding site. The binding site of Smyd3 consists mainly of a deep and narrow pocket, while those of Smyd1 and Smyd2 consist of a comparable pocket and a long groove. In addition, Smyd2, which has lysine methyltransferase activity on histone H3-lysine 36, exhibits substantial differences in the wall of the substrate-binding pocket compared with those of Smyd1 and Smyd3 which have activity specifically on histone H3-lysine 4. The differences in the substrate-binding site might account for the observed divergence in the specificity and methylation state of the substrates. Further modeling study of Smyd2 in complex with a p53 peptide indicates that mono-methylation of p53-Lys(372) might result in steric conflict of the methyl group with the surrounding residues of Smyd2, providing a structural explanation for the inhibitory effect of the SET7/9-mediated mono-methylation of p53-Lys(372) on the Smyd2-mediated methylation of p53-Lys(370).

-	~~==Function==~~	+	Structure of human lysine methyltransferase Smyd2 reveals insights into the substrate divergence in Smyd proteins.,Xu S, Zhong C, Zhang T, Ding J J Mol Cell Biol. 2011 Jul 1. PMID:21724641<ref>PMID:21724641</ref>
-	~~[[http://www.uniprot.org/uniprot/SMYD2_HUMAN SMYD2_HUMAN]] Protein-~~lysine N-methyltransferase ~~that methylates both histones and non-histone~~ proteins. Specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). Has also methyltransferase activity toward non-histone proteins such as p53/TP53 and RB1. Monomethylates 'Lys-370' of p53/TP53, ~~leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53~~. ~~Monomethylates 'Lys-860' of RB1/RB~~.~~<ref>~~PMID:~~17108971</ref> <ref>PMID:17805299</ref> <ref>PMID:18065756</ref>~~ <ref>PMID:~~20870719~~</ref>	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[3rib]] 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=3RIB OCA].~~	+	</div>

-	==~~Reference~~==	+	==See Also==
-	~~<ref group~~=~~"xtra">PMID:021724641</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	*[[Histone methyltransferase\|Histone methyltransferase]]
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Ding, J.]]	+	[[Category: Ding, J]]
-	[[Category: Xu, S.]]	+	[[Category: Xu, S]]
-	[[Category: Zhang, T.]]	+	[[Category: Zhang, T]]
-	[[Category: Zhong, C.]]	+	[[Category: Zhong, C]]
	[[Category: H3k36]]		[[Category: H3k36]]
	[[Category: H3k4]]		[[Category: H3k4]]

OCA at 07:36, 30 June 2013

OCA — Sun, 30 Jun 2013 07:36:12 GMT

←Older revision		Revision as of 07:36, 30 June 2013
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-	[[Image:3rib.png\|left\|200px]]
-
	{{STRUCTURE_3rib\| PDB=3rib \| SCENE= }}		{{STRUCTURE_3rib\| PDB=3rib \| SCENE= }}
-
	===Human lysine methyltransferase Smyd2 in complex with AdoHcy===		===Human lysine methyltransferase Smyd2 in complex with AdoHcy===
-
	{{ABSTRACT_PUBMED_21724641}}		{{ABSTRACT_PUBMED_21724641}}
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/SMYD2_HUMAN SMYD2_HUMAN]] Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins. Specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). Has also methyltransferase activity toward non-histone proteins such as p53/TP53 and RB1. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates 'Lys-860' of RB1/RB.<ref>PMID:17108971</ref> <ref>PMID:17805299</ref> <ref>PMID:18065756</ref> <ref>PMID:20870719</ref>

	==About this Structure==		==About this Structure==
	[[3rib]] 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=3RIB OCA].		[[3rib]] 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=3RIB OCA].
-
-	==See Also==
-	*[[Histone methyltransferase\|Histone methyltransferase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:021724641</ref><references group="xtra"/>	+	<ref group="xtra">PMID:021724641</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Ding, J.]]		[[Category: Ding, J.]]

OCA at 10:28, 20 October 2012

OCA — Sat, 20 Oct 2012 10:28:06 GMT

←Older revision		Revision as of 10:28, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3rib]] is a 2 chain structure ~~of [[Histone methyltransferase]]~~ 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=3RIB OCA].	+	[[3rib]] 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=3RIB OCA].

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

OCA at 02:13, 26 July 2012

OCA — Thu, 26 Jul 2012 02:13:07 GMT

←Older revision		Revision as of 02:13, 26 July 2012
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	[[Image:3rib.png\|left\|200px]]		[[Image:3rib.png\|left\|200px]]

-	<!--
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	{{STRUCTURE_3rib\| PDB=3rib \| SCENE= }}		{{STRUCTURE_3rib\| PDB=3rib \| SCENE= }}

	===Human lysine methyltransferase Smyd2 in complex with AdoHcy===		===Human lysine methyltransferase Smyd2 in complex with AdoHcy===

-
-	<!--
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	==About this Structure==		==About this Structure==
-	[[3rib]] 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=3RIB OCA].	+	[[3rib]] is a 2 chain structure of [[Histone methyltransferase]] 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=3RIB OCA].
		+
		+	==See Also==
		+	*[[Histone methyltransferase\|Histone methyltransferase]]

	==Reference==		==Reference==

OCA at 06:15, 27 July 2011

OCA — Wed, 27 Jul 2011 06:15:30 GMT

←Older revision		Revision as of 06:15, 27 July 2011
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-	[[Image:3rib.~~jpg~~\|left\|200px]]	+	[[Image:3rib.png\|left\|200px]]

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